Phosphorus in PDB 1a8r: Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp
Enzymatic activity of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp
All present enzymatic activity of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp:
3.5.4.16;
Protein crystallography data
The structure of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp, PDB code: 1a8r
was solved by
G.Auerbach,
H.Nar,
A.Bracher,
A.Bacher,
R.Huber,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
8.00 /
2.10
|
Space group
|
C 2 2 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
314.950,
219.140,
131.410,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20 /
24.6
|
Phosphorus Binding Sites:
Phosphorus binding site 1 out
of 45 in 1a8r
Go back to
Phosphorus Binding Sites List in 1a8r
Phosphorus binding site 1 out
of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 1 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:P401
b:29.4
occ:1.00
|
PG
|
A:GTP401
|
0.0
|
29.4
|
1.0
|
O1G
|
A:GTP401
|
1.5
|
29.2
|
1.0
|
O2G
|
A:GTP401
|
1.5
|
26.9
|
1.0
|
O3G
|
A:GTP401
|
1.6
|
29.0
|
1.0
|
O3B
|
A:GTP401
|
1.6
|
36.6
|
1.0
|
PB
|
A:GTP401
|
2.9
|
30.6
|
1.0
|
NH1
|
B:ARG139
|
3.1
|
37.8
|
1.0
|
O1B
|
A:GTP401
|
3.3
|
23.2
|
1.0
|
OG
|
B:SER135
|
3.4
|
37.8
|
1.0
|
O2B
|
A:GTP401
|
3.4
|
26.7
|
1.0
|
NH2
|
A:ARG185
|
3.5
|
44.6
|
1.0
|
NZ
|
B:LYS136
|
3.7
|
27.7
|
1.0
|
NH1
|
A:ARG185
|
3.8
|
38.2
|
1.0
|
O
|
A:HOH450
|
3.9
|
25.7
|
1.0
|
CZ
|
A:ARG185
|
4.1
|
37.1
|
1.0
|
O3A
|
A:GTP401
|
4.1
|
26.7
|
1.0
|
O
|
A:HOH453
|
4.2
|
38.4
|
1.0
|
O
|
A:HOH422
|
4.3
|
50.3
|
1.0
|
CB
|
B:SER135
|
4.3
|
33.4
|
1.0
|
CZ
|
B:ARG139
|
4.4
|
30.1
|
1.0
|
C3'
|
A:GTP401
|
4.4
|
25.2
|
1.0
|
O3'
|
A:GTP401
|
4.5
|
18.9
|
1.0
|
CE
|
B:LYS136
|
4.6
|
29.4
|
1.0
|
O1A
|
A:GTP401
|
4.6
|
20.9
|
1.0
|
O5'
|
A:GTP401
|
4.7
|
35.6
|
1.0
|
CD
|
B:ARG139
|
4.7
|
26.6
|
1.0
|
PA
|
A:GTP401
|
4.8
|
29.4
|
1.0
|
NE
|
B:ARG139
|
5.0
|
33.7
|
1.0
|
CE1
|
A:HIS113
|
5.0
|
27.9
|
1.0
|
|
Phosphorus binding site 2 out
of 45 in 1a8r
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Phosphorus Binding Sites List in 1a8r
Phosphorus binding site 2 out
of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 2 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:P401
b:30.6
occ:1.00
|
PB
|
A:GTP401
|
0.0
|
30.6
|
1.0
|
O1B
|
A:GTP401
|
1.4
|
23.2
|
1.0
|
O2B
|
A:GTP401
|
1.4
|
26.7
|
1.0
|
O3A
|
A:GTP401
|
1.6
|
26.7
|
1.0
|
O3B
|
A:GTP401
|
1.6
|
36.6
|
1.0
|
PA
|
A:GTP401
|
2.9
|
29.4
|
1.0
|
PG
|
A:GTP401
|
2.9
|
29.4
|
1.0
|
O1A
|
A:GTP401
|
3.1
|
20.9
|
1.0
|
O1G
|
A:GTP401
|
3.1
|
29.2
|
1.0
|
O5'
|
A:GTP401
|
3.6
|
35.6
|
1.0
|
NH2
|
A:ARG185
|
3.7
|
44.6
|
1.0
|
O3G
|
A:GTP401
|
3.7
|
29.0
|
1.0
|
NE2
|
A:HIS113
|
3.9
|
19.7
|
1.0
|
O
|
A:HOH443
|
4.0
|
52.0
|
1.0
|
O2G
|
A:GTP401
|
4.0
|
26.9
|
1.0
|
CE1
|
A:HIS113
|
4.0
|
27.9
|
1.0
|
O2A
|
A:GTP401
|
4.1
|
33.2
|
1.0
|
C5'
|
A:GTP401
|
4.2
|
30.1
|
1.0
|
O
|
A:HOH422
|
4.3
|
50.3
|
1.0
|
NZ
|
B:LYS136
|
4.4
|
27.7
|
1.0
|
CZ
|
A:ARG185
|
4.6
|
37.1
|
1.0
|
C3'
|
A:GTP401
|
4.9
|
25.2
|
1.0
|
O
|
A:HOH454
|
4.9
|
33.2
|
1.0
|
NH1
|
A:ARG185
|
5.0
|
38.2
|
1.0
|
|
Phosphorus binding site 3 out
of 45 in 1a8r
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Phosphorus Binding Sites List in 1a8r
Phosphorus binding site 3 out
of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 3 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:P401
b:29.4
occ:1.00
|
PA
|
A:GTP401
|
0.0
|
29.4
|
1.0
|
O2A
|
A:GTP401
|
1.5
|
33.2
|
1.0
|
O1A
|
A:GTP401
|
1.5
|
20.9
|
1.0
|
O5'
|
A:GTP401
|
1.6
|
35.6
|
1.0
|
O3A
|
A:GTP401
|
1.7
|
26.7
|
1.0
|
C5'
|
A:GTP401
|
2.7
|
30.1
|
1.0
|
PB
|
A:GTP401
|
2.9
|
30.6
|
1.0
|
O3B
|
A:GTP401
|
3.2
|
36.6
|
1.0
|
O1B
|
A:GTP401
|
3.3
|
23.2
|
1.0
|
CG2
|
B:THR87
|
3.6
|
41.6
|
1.0
|
C4'
|
A:GTP401
|
3.9
|
26.0
|
1.0
|
OG1
|
B:THR87
|
3.9
|
53.7
|
1.0
|
O2B
|
A:GTP401
|
4.0
|
26.7
|
1.0
|
NZ
|
B:LYS136
|
4.2
|
27.7
|
1.0
|
CB
|
B:THR87
|
4.3
|
40.0
|
1.0
|
C3'
|
A:GTP401
|
4.3
|
25.2
|
1.0
|
CE
|
B:LYS136
|
4.4
|
29.4
|
1.0
|
O
|
A:HOH443
|
4.4
|
52.0
|
1.0
|
PG
|
A:GTP401
|
4.8
|
29.4
|
1.0
|
O3'
|
A:GTP401
|
4.8
|
18.9
|
1.0
|
|
Phosphorus binding site 4 out
of 45 in 1a8r
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Phosphorus Binding Sites List in 1a8r
Phosphorus binding site 4 out
of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 4 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:P402
b:26.9
occ:1.00
|
PG
|
B:GTP402
|
0.0
|
26.9
|
1.0
|
O2G
|
B:GTP402
|
1.5
|
38.7
|
1.0
|
O1G
|
B:GTP402
|
1.5
|
23.4
|
1.0
|
O3G
|
B:GTP402
|
1.6
|
26.8
|
1.0
|
O3B
|
B:GTP402
|
1.6
|
31.4
|
1.0
|
PB
|
B:GTP402
|
2.9
|
31.6
|
1.0
|
NH1
|
C:ARG139
|
3.0
|
41.0
|
1.0
|
O2B
|
B:GTP402
|
3.3
|
31.7
|
1.0
|
O1B
|
B:GTP402
|
3.4
|
31.5
|
1.0
|
OG
|
C:SER135
|
3.5
|
23.9
|
1.0
|
NH2
|
B:ARG185
|
3.6
|
29.4
|
1.0
|
NZ
|
C:LYS136
|
3.7
|
23.0
|
1.0
|
O
|
B:HOH553
|
3.8
|
27.8
|
1.0
|
NH1
|
B:ARG185
|
3.8
|
22.8
|
1.0
|
O
|
B:HOH556
|
4.0
|
31.2
|
1.0
|
O3A
|
B:GTP402
|
4.1
|
33.7
|
1.0
|
O
|
B:HOH515
|
4.1
|
55.6
|
1.0
|
CZ
|
C:ARG139
|
4.1
|
34.4
|
1.0
|
CZ
|
B:ARG185
|
4.2
|
25.1
|
1.0
|
CB
|
C:SER135
|
4.5
|
21.5
|
1.0
|
C3'
|
B:GTP402
|
4.5
|
24.7
|
1.0
|
CD
|
C:ARG139
|
4.6
|
26.5
|
1.0
|
CE
|
C:LYS136
|
4.6
|
25.8
|
1.0
|
O1A
|
B:GTP402
|
4.7
|
30.1
|
1.0
|
O3'
|
B:GTP402
|
4.7
|
18.8
|
1.0
|
NE
|
C:ARG139
|
4.7
|
39.7
|
1.0
|
O5'
|
B:GTP402
|
4.8
|
22.7
|
1.0
|
PA
|
B:GTP402
|
4.9
|
28.5
|
1.0
|
CA
|
B:GLY186
|
4.9
|
27.4
|
1.0
|
CE1
|
B:HIS113
|
4.9
|
26.1
|
1.0
|
|
Phosphorus binding site 5 out
of 45 in 1a8r
Go back to
Phosphorus Binding Sites List in 1a8r
Phosphorus binding site 5 out
of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 5 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:P402
b:31.6
occ:1.00
|
PB
|
B:GTP402
|
0.0
|
31.6
|
1.0
|
O1B
|
B:GTP402
|
1.4
|
31.5
|
1.0
|
O2B
|
B:GTP402
|
1.4
|
31.7
|
1.0
|
O3B
|
B:GTP402
|
1.6
|
31.4
|
1.0
|
O3A
|
B:GTP402
|
1.6
|
33.7
|
1.0
|
PG
|
B:GTP402
|
2.9
|
26.9
|
1.0
|
PA
|
B:GTP402
|
2.9
|
28.5
|
1.0
|
O1G
|
B:GTP402
|
3.1
|
23.4
|
1.0
|
O1A
|
B:GTP402
|
3.2
|
30.1
|
1.0
|
O5'
|
B:GTP402
|
3.6
|
22.7
|
1.0
|
NH2
|
B:ARG185
|
3.7
|
29.4
|
1.0
|
O3G
|
B:GTP402
|
3.7
|
26.8
|
1.0
|
NE2
|
B:HIS113
|
3.8
|
27.6
|
1.0
|
O2G
|
B:GTP402
|
3.9
|
38.7
|
1.0
|
CE1
|
B:HIS113
|
4.0
|
26.1
|
1.0
|
O
|
B:HOH545
|
4.1
|
63.5
|
1.0
|
O2A
|
B:GTP402
|
4.1
|
36.5
|
1.0
|
C5'
|
B:GTP402
|
4.1
|
27.3
|
1.0
|
O
|
B:HOH515
|
4.2
|
55.6
|
1.0
|
NZ
|
C:LYS136
|
4.2
|
23.0
|
1.0
|
CZ
|
B:ARG185
|
4.6
|
25.1
|
1.0
|
O
|
B:HOH557
|
4.8
|
28.0
|
1.0
|
NH1
|
B:ARG185
|
4.8
|
22.8
|
1.0
|
C3'
|
B:GTP402
|
5.0
|
24.7
|
1.0
|
|
Phosphorus binding site 6 out
of 45 in 1a8r
Go back to
Phosphorus Binding Sites List in 1a8r
Phosphorus binding site 6 out
of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 6 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:P402
b:28.5
occ:1.00
|
PA
|
B:GTP402
|
0.0
|
28.5
|
1.0
|
O2A
|
B:GTP402
|
1.4
|
36.5
|
1.0
|
O1A
|
B:GTP402
|
1.5
|
30.1
|
1.0
|
O5'
|
B:GTP402
|
1.6
|
22.7
|
1.0
|
O3A
|
B:GTP402
|
1.7
|
33.7
|
1.0
|
C5'
|
B:GTP402
|
2.7
|
27.3
|
1.0
|
PB
|
B:GTP402
|
2.9
|
31.6
|
1.0
|
O3B
|
B:GTP402
|
3.3
|
31.4
|
1.0
|
O1B
|
B:GTP402
|
3.3
|
31.5
|
1.0
|
CG2
|
C:THR87
|
3.7
|
25.1
|
1.0
|
C4'
|
B:GTP402
|
3.8
|
22.9
|
1.0
|
NZ
|
C:LYS136
|
4.0
|
23.0
|
1.0
|
O2B
|
B:GTP402
|
4.1
|
31.7
|
1.0
|
OG1
|
C:THR87
|
4.1
|
41.8
|
1.0
|
CE
|
C:LYS136
|
4.3
|
25.8
|
1.0
|
O
|
B:HOH545
|
4.4
|
63.5
|
1.0
|
C3'
|
B:GTP402
|
4.4
|
24.7
|
1.0
|
CB
|
C:THR87
|
4.5
|
37.9
|
1.0
|
PG
|
B:GTP402
|
4.9
|
26.9
|
1.0
|
O3'
|
B:GTP402
|
4.9
|
18.8
|
1.0
|
|
Phosphorus binding site 7 out
of 45 in 1a8r
Go back to
Phosphorus Binding Sites List in 1a8r
Phosphorus binding site 7 out
of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 7 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:P403
b:25.5
occ:1.00
|
PG
|
C:GTP403
|
0.0
|
25.5
|
1.0
|
O1G
|
C:GTP403
|
1.5
|
28.6
|
1.0
|
O2G
|
C:GTP403
|
1.5
|
24.1
|
1.0
|
O3G
|
C:GTP403
|
1.6
|
31.6
|
1.0
|
O3B
|
C:GTP403
|
1.7
|
27.5
|
1.0
|
PB
|
C:GTP403
|
3.0
|
28.7
|
1.0
|
NH1
|
D:ARG139
|
3.1
|
26.4
|
1.0
|
O1B
|
C:GTP403
|
3.4
|
34.1
|
1.0
|
OG
|
D:SER135
|
3.5
|
35.1
|
1.0
|
O2B
|
C:GTP403
|
3.5
|
32.4
|
1.0
|
NH1
|
C:ARG185
|
3.6
|
38.5
|
1.0
|
O
|
C:HOH573
|
3.7
|
30.0
|
1.0
|
NH2
|
C:ARG185
|
3.8
|
43.3
|
1.0
|
NZ
|
D:LYS136
|
3.9
|
19.9
|
1.0
|
O
|
C:HOH576
|
3.9
|
28.4
|
1.0
|
CZ
|
C:ARG185
|
4.1
|
37.5
|
1.0
|
O3A
|
C:GTP403
|
4.2
|
26.2
|
1.0
|
O
|
C:HOH545
|
4.2
|
52.8
|
1.0
|
CB
|
D:SER135
|
4.3
|
26.1
|
1.0
|
CZ
|
D:ARG139
|
4.4
|
25.4
|
1.0
|
C3'
|
C:GTP403
|
4.5
|
27.1
|
1.0
|
O1A
|
C:GTP403
|
4.6
|
30.9
|
1.0
|
CE
|
D:LYS136
|
4.6
|
17.4
|
1.0
|
O3'
|
C:GTP403
|
4.7
|
20.4
|
1.0
|
CD
|
D:ARG139
|
4.7
|
19.4
|
1.0
|
O5'
|
C:GTP403
|
4.8
|
31.7
|
1.0
|
CE1
|
C:HIS113
|
4.9
|
26.7
|
1.0
|
PA
|
C:GTP403
|
4.9
|
29.6
|
1.0
|
CA
|
C:GLY186
|
4.9
|
25.1
|
1.0
|
|
Phosphorus binding site 8 out
of 45 in 1a8r
Go back to
Phosphorus Binding Sites List in 1a8r
Phosphorus binding site 8 out
of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 8 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:P403
b:28.7
occ:1.00
|
PB
|
C:GTP403
|
0.0
|
28.7
|
1.0
|
O2B
|
C:GTP403
|
1.4
|
32.4
|
1.0
|
O1B
|
C:GTP403
|
1.5
|
34.1
|
1.0
|
O3A
|
C:GTP403
|
1.6
|
26.2
|
1.0
|
O3B
|
C:GTP403
|
1.6
|
27.5
|
1.0
|
PA
|
C:GTP403
|
2.9
|
29.6
|
1.0
|
PG
|
C:GTP403
|
3.0
|
25.5
|
1.0
|
O1A
|
C:GTP403
|
3.1
|
30.9
|
1.0
|
O1G
|
C:GTP403
|
3.2
|
28.6
|
1.0
|
O5'
|
C:GTP403
|
3.6
|
31.7
|
1.0
|
NH2
|
C:ARG185
|
3.7
|
43.3
|
1.0
|
O3G
|
C:GTP403
|
3.8
|
31.6
|
1.0
|
NE2
|
C:HIS113
|
3.9
|
24.2
|
1.0
|
CE1
|
C:HIS113
|
4.0
|
26.7
|
1.0
|
O
|
C:HOH566
|
4.1
|
51.5
|
1.0
|
O2A
|
C:GTP403
|
4.1
|
27.5
|
1.0
|
O2G
|
C:GTP403
|
4.1
|
24.1
|
1.0
|
O
|
C:HOH545
|
4.1
|
52.8
|
1.0
|
C5'
|
C:GTP403
|
4.2
|
32.6
|
1.0
|
NZ
|
D:LYS136
|
4.4
|
19.9
|
1.0
|
CZ
|
C:ARG185
|
4.5
|
37.5
|
1.0
|
NH1
|
C:ARG185
|
4.8
|
38.5
|
1.0
|
O
|
C:HOH577
|
4.9
|
38.2
|
1.0
|
C3'
|
C:GTP403
|
4.9
|
27.1
|
1.0
|
|
Phosphorus binding site 9 out
of 45 in 1a8r
Go back to
Phosphorus Binding Sites List in 1a8r
Phosphorus binding site 9 out
of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 9 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:P403
b:29.6
occ:1.00
|
PA
|
C:GTP403
|
0.0
|
29.6
|
1.0
|
O2A
|
C:GTP403
|
1.5
|
27.5
|
1.0
|
O1A
|
C:GTP403
|
1.5
|
30.9
|
1.0
|
O5'
|
C:GTP403
|
1.6
|
31.7
|
1.0
|
O3A
|
C:GTP403
|
1.7
|
26.2
|
1.0
|
C5'
|
C:GTP403
|
2.7
|
32.6
|
1.0
|
PB
|
C:GTP403
|
2.9
|
28.7
|
1.0
|
O3B
|
C:GTP403
|
3.3
|
27.5
|
1.0
|
O1B
|
C:GTP403
|
3.3
|
34.1
|
1.0
|
CG2
|
D:THR87
|
3.7
|
35.4
|
1.0
|
C4'
|
C:GTP403
|
3.8
|
26.0
|
1.0
|
O2B
|
C:GTP403
|
4.0
|
32.4
|
1.0
|
NZ
|
D:LYS136
|
4.2
|
19.9
|
1.0
|
OG1
|
D:THR87
|
4.3
|
50.1
|
1.0
|
O
|
C:HOH566
|
4.3
|
51.5
|
1.0
|
C3'
|
C:GTP403
|
4.3
|
27.1
|
1.0
|
CE
|
D:LYS136
|
4.4
|
17.4
|
1.0
|
CB
|
D:THR87
|
4.5
|
33.6
|
1.0
|
O3'
|
C:GTP403
|
4.8
|
20.4
|
1.0
|
PG
|
C:GTP403
|
4.9
|
25.5
|
1.0
|
|
Phosphorus binding site 10 out
of 45 in 1a8r
Go back to
Phosphorus Binding Sites List in 1a8r
Phosphorus binding site 10 out
of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 10 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:P404
b:28.4
occ:1.00
|
PG
|
D:GTP404
|
0.0
|
28.4
|
1.0
|
O1G
|
D:GTP404
|
1.5
|
28.6
|
1.0
|
O2G
|
D:GTP404
|
1.5
|
35.6
|
1.0
|
O3G
|
D:GTP404
|
1.6
|
33.2
|
1.0
|
O3B
|
D:GTP404
|
1.7
|
41.8
|
1.0
|
PB
|
D:GTP404
|
2.9
|
36.1
|
1.0
|
NH1
|
E:ARG139
|
3.1
|
39.8
|
1.0
|
O1B
|
D:GTP404
|
3.3
|
31.7
|
1.0
|
O2B
|
D:GTP404
|
3.4
|
33.0
|
1.0
|
NH2
|
D:ARG185
|
3.4
|
43.9
|
1.0
|
OG
|
E:SER135
|
3.5
|
36.5
|
1.0
|
NH1
|
D:ARG185
|
3.7
|
34.7
|
1.0
|
NZ
|
E:LYS136
|
3.7
|
28.3
|
1.0
|
O
|
D:HOH572
|
3.8
|
26.5
|
1.0
|
O
|
D:HOH544
|
3.9
|
65.0
|
1.0
|
CZ
|
D:ARG185
|
4.0
|
33.8
|
1.0
|
O3A
|
D:GTP404
|
4.1
|
32.4
|
1.0
|
O
|
D:HOH575
|
4.2
|
35.5
|
1.0
|
CZ
|
E:ARG139
|
4.3
|
33.3
|
1.0
|
CB
|
E:SER135
|
4.4
|
30.7
|
1.0
|
C3'
|
D:GTP404
|
4.5
|
31.1
|
1.0
|
CE
|
E:LYS136
|
4.5
|
28.1
|
1.0
|
O1A
|
D:GTP404
|
4.6
|
31.6
|
1.0
|
O3'
|
D:GTP404
|
4.7
|
28.2
|
1.0
|
O5'
|
D:GTP404
|
4.7
|
33.2
|
1.0
|
CD
|
E:ARG139
|
4.7
|
29.6
|
1.0
|
PA
|
D:GTP404
|
4.9
|
32.9
|
1.0
|
NE
|
E:ARG139
|
4.9
|
37.8
|
1.0
|
CE1
|
D:HIS113
|
4.9
|
25.3
|
1.0
|
CA
|
D:GLY186
|
5.0
|
37.2
|
1.0
|
|
Reference:
J.Rebelo,
G.Auerbach,
G.Bader,
A.Bracher,
H.Nar,
C.Hosl,
N.Schramek,
J.Kaiser,
A.Bacher,
R.Huber,
M.Fischer.
Biosynthesis of Pteridines. Reaction Mechanism of Gtp Cyclohydrolase I. J.Mol.Biol. V. 326 503 2003.
ISSN: ISSN 0022-2836
PubMed: 12559918
DOI: 10.1016/S0022-2836(02)01303-7
Page generated: Fri Sep 25 12:27:57 2020
|