Phosphorus in PDB 1aax: Crystal Structure of Protein Tyrosine Phosphatase 1B Complexed with Two Bis(Para-Phosphophenyl)Methane (Bppm) Molecules
Enzymatic activity of Crystal Structure of Protein Tyrosine Phosphatase 1B Complexed with Two Bis(Para-Phosphophenyl)Methane (Bppm) Molecules
All present enzymatic activity of Crystal Structure of Protein Tyrosine Phosphatase 1B Complexed with Two Bis(Para-Phosphophenyl)Methane (Bppm) Molecules:
3.1.3.48;
Protein crystallography data
The structure of Crystal Structure of Protein Tyrosine Phosphatase 1B Complexed with Two Bis(Para-Phosphophenyl)Methane (Bppm) Molecules, PDB code: 1aax
was solved by
Y.A.Puius,
Y.Zhao,
M.Sullivan,
D.Lawrence,
S.C.Almo,
Z.-Y.Zhang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
22.00 /
1.90
|
Space group
|
P 31 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
88.369,
88.369,
104.532,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
18.2 /
n/a
|
Phosphorus Binding Sites:
The binding sites of Phosphorus atom in the Crystal Structure of Protein Tyrosine Phosphatase 1B Complexed with Two Bis(Para-Phosphophenyl)Methane (Bppm) Molecules
(pdb code 1aax). This binding sites where shown within
5.0 Angstroms radius around Phosphorus atom.
In total 4 binding sites of Phosphorus where determined in the
Crystal Structure of Protein Tyrosine Phosphatase 1B Complexed with Two Bis(Para-Phosphophenyl)Methane (Bppm) Molecules, PDB code: 1aax:
Jump to Phosphorus binding site number:
1;
2;
3;
4;
Phosphorus binding site 1 out
of 4 in 1aax
Go back to
Phosphorus Binding Sites List in 1aax
Phosphorus binding site 1 out
of 4 in the Crystal Structure of Protein Tyrosine Phosphatase 1B Complexed with Two Bis(Para-Phosphophenyl)Methane (Bppm) Molecules
 Mono view
 Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 1 of Crystal Structure of Protein Tyrosine Phosphatase 1B Complexed with Two Bis(Para-Phosphophenyl)Methane (Bppm) Molecules within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:P402
b:2.7
occ:0.54
|
PA
|
A:BPM402
|
0.0
|
2.7
|
0.5
|
O3A
|
A:BPM402
|
1.4
|
3.7
|
0.5
|
O4A
|
A:BPM402
|
1.4
|
2.0
|
0.5
|
O2A
|
A:BPM402
|
1.4
|
2.3
|
0.5
|
O1A
|
A:BPM402
|
1.5
|
2.8
|
0.5
|
C4A
|
A:BPM402
|
2.5
|
2.5
|
0.5
|
C3A
|
A:BPM402
|
3.3
|
4.1
|
0.5
|
OG
|
A:SER215
|
3.4
|
17.7
|
1.0
|
O
|
A:HOH528
|
3.5
|
20.0
|
1.0
|
C5A
|
A:BPM402
|
3.5
|
3.1
|
0.5
|
CB
|
A:SER215
|
3.7
|
16.0
|
1.0
|
N
|
A:GLY220
|
3.8
|
19.7
|
1.0
|
NE
|
A:ARG221
|
3.8
|
15.6
|
1.0
|
NH2
|
A:ARG221
|
3.8
|
13.3
|
1.0
|
N
|
A:ALA217
|
3.9
|
11.9
|
1.0
|
N
|
A:ARG221
|
4.1
|
15.2
|
1.0
|
CA
|
A:GLY220
|
4.1
|
15.9
|
1.0
|
N
|
A:SER216
|
4.1
|
14.6
|
1.0
|
CB
|
A:ALA217
|
4.2
|
13.2
|
1.0
|
CZ
|
A:ARG221
|
4.3
|
15.2
|
1.0
|
N
|
A:GLY218
|
4.4
|
15.9
|
1.0
|
N
|
A:ILE219
|
4.6
|
14.9
|
1.0
|
CA
|
A:ALA217
|
4.6
|
13.1
|
1.0
|
C2A
|
A:BPM402
|
4.6
|
4.4
|
0.5
|
C
|
A:GLY220
|
4.7
|
15.1
|
1.0
|
C6A
|
A:BPM402
|
4.8
|
3.7
|
0.5
|
CB
|
A:SER216
|
4.8
|
9.7
|
1.0
|
CG
|
A:ARG221
|
4.8
|
16.0
|
1.0
|
CA
|
A:SER216
|
4.9
|
11.4
|
1.0
|
C
|
A:SER216
|
4.9
|
12.6
|
1.0
|
CA
|
A:SER215
|
4.9
|
15.7
|
1.0
|
CB
|
A:ARG221
|
4.9
|
15.4
|
1.0
|
C
|
A:ILE219
|
4.9
|
16.9
|
1.0
|
CD
|
A:ARG221
|
4.9
|
14.7
|
1.0
|
C
|
A:SER215
|
4.9
|
15.2
|
1.0
|
C
|
A:ALA217
|
5.0
|
15.1
|
1.0
|
CG1
|
A:ILE219
|
5.0
|
16.4
|
1.0
|
|
Phosphorus binding site 2 out
of 4 in 1aax
Go back to
Phosphorus Binding Sites List in 1aax
Phosphorus binding site 2 out
of 4 in the Crystal Structure of Protein Tyrosine Phosphatase 1B Complexed with Two Bis(Para-Phosphophenyl)Methane (Bppm) Molecules
 Mono view
 Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 2 of Crystal Structure of Protein Tyrosine Phosphatase 1B Complexed with Two Bis(Para-Phosphophenyl)Methane (Bppm) Molecules within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:P402
b:27.2
occ:0.54
|
PB
|
A:BPM402
|
0.0
|
27.2
|
0.5
|
O3B
|
A:BPM403
|
1.4
|
41.4
|
0.5
|
O2B
|
A:BPM402
|
1.5
|
31.0
|
0.5
|
O4B
|
A:BPM402
|
1.5
|
28.6
|
0.5
|
O3B
|
A:BPM402
|
1.5
|
31.3
|
0.5
|
O1B
|
A:BPM402
|
1.5
|
25.3
|
0.5
|
O4B
|
A:BPM403
|
1.5
|
39.9
|
0.5
|
PB
|
A:BPM403
|
1.6
|
41.1
|
0.5
|
O2B
|
A:BPM403
|
2.5
|
41.5
|
0.5
|
C4B
|
A:BPM402
|
2.7
|
17.9
|
0.5
|
O1B
|
A:BPM403
|
2.9
|
32.2
|
0.5
|
C5B
|
A:BPM402
|
3.3
|
14.7
|
0.5
|
C3B
|
A:BPM402
|
3.8
|
15.8
|
0.5
|
C4B
|
A:BPM403
|
3.9
|
26.8
|
0.5
|
O
|
A:HOH708
|
4.1
|
45.9
|
1.0
|
C5B
|
A:BPM403
|
4.3
|
23.9
|
0.5
|
C6B
|
A:BPM402
|
4.7
|
13.2
|
0.5
|
C3B
|
A:BPM403
|
4.8
|
25.3
|
0.5
|
|
Phosphorus binding site 3 out
of 4 in 1aax
Go back to
Phosphorus Binding Sites List in 1aax
Phosphorus binding site 3 out
of 4 in the Crystal Structure of Protein Tyrosine Phosphatase 1B Complexed with Two Bis(Para-Phosphophenyl)Methane (Bppm) Molecules
 Mono view
 Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 3 of Crystal Structure of Protein Tyrosine Phosphatase 1B Complexed with Two Bis(Para-Phosphophenyl)Methane (Bppm) Molecules within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:P403
b:12.5
occ:0.46
|
PA
|
A:BPM403
|
0.0
|
12.5
|
0.5
|
O3A
|
A:BPM403
|
1.4
|
10.3
|
0.5
|
O4A
|
A:BPM403
|
1.4
|
9.4
|
0.5
|
O2A
|
A:BPM403
|
1.5
|
13.4
|
0.5
|
O1A
|
A:BPM403
|
1.5
|
9.8
|
0.5
|
C4A
|
A:BPM403
|
2.5
|
9.5
|
0.5
|
C5A
|
A:BPM403
|
3.0
|
10.2
|
0.5
|
O
|
A:HOH520
|
3.5
|
17.8
|
1.0
|
O
|
A:HOH529
|
3.7
|
24.1
|
1.0
|
NH1
|
A:ARG254
|
3.7
|
17.2
|
1.0
|
NH2
|
A:ARG24
|
3.7
|
45.7
|
1.0
|
C3A
|
A:BPM403
|
3.7
|
9.1
|
0.5
|
NE
|
A:ARG24
|
3.9
|
35.4
|
1.0
|
CZ
|
A:ARG24
|
4.3
|
43.9
|
1.0
|
C6A
|
A:BPM403
|
4.4
|
13.1
|
0.5
|
N
|
A:GLY259
|
4.6
|
17.2
|
1.0
|
O
|
A:ARG24
|
4.7
|
32.2
|
1.0
|
CA
|
A:GLY259
|
4.7
|
17.6
|
1.0
|
CB
|
A:ARG24
|
4.8
|
27.0
|
1.0
|
O
|
A:HOH679
|
4.8
|
37.4
|
1.0
|
CZ
|
A:ARG254
|
4.8
|
20.1
|
1.0
|
C2A
|
A:BPM403
|
4.9
|
9.7
|
0.5
|
|
Phosphorus binding site 4 out
of 4 in 1aax
Go back to
Phosphorus Binding Sites List in 1aax
Phosphorus binding site 4 out
of 4 in the Crystal Structure of Protein Tyrosine Phosphatase 1B Complexed with Two Bis(Para-Phosphophenyl)Methane (Bppm) Molecules
 Mono view
 Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 4 of Crystal Structure of Protein Tyrosine Phosphatase 1B Complexed with Two Bis(Para-Phosphophenyl)Methane (Bppm) Molecules within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:P403
b:41.1
occ:0.46
|
PB
|
A:BPM403
|
0.0
|
41.1
|
0.5
|
O3B
|
A:BPM402
|
1.3
|
31.3
|
0.5
|
O1B
|
A:BPM403
|
1.5
|
32.2
|
0.5
|
O4B
|
A:BPM403
|
1.5
|
39.9
|
0.5
|
O3B
|
A:BPM403
|
1.5
|
41.4
|
0.5
|
O2B
|
A:BPM403
|
1.5
|
41.5
|
0.5
|
PB
|
A:BPM402
|
1.6
|
27.2
|
0.5
|
O1B
|
A:BPM402
|
1.6
|
25.3
|
0.5
|
C4B
|
A:BPM402
|
2.3
|
17.9
|
0.5
|
C4B
|
A:BPM403
|
2.3
|
26.8
|
0.5
|
O4B
|
A:BPM402
|
2.7
|
28.6
|
0.5
|
O2B
|
A:BPM402
|
2.8
|
31.0
|
0.5
|
C3B
|
A:BPM402
|
3.0
|
15.8
|
0.5
|
C5B
|
A:BPM403
|
3.0
|
23.9
|
0.5
|
C3B
|
A:BPM403
|
3.2
|
25.3
|
0.5
|
C5B
|
A:BPM402
|
3.2
|
14.7
|
0.5
|
O
|
A:HOH708
|
4.0
|
45.9
|
1.0
|
C2B
|
A:BPM402
|
4.2
|
12.8
|
0.5
|
C6B
|
A:BPM403
|
4.3
|
22.4
|
0.5
|
C2B
|
A:BPM403
|
4.4
|
24.7
|
0.5
|
C6B
|
A:BPM402
|
4.4
|
13.2
|
0.5
|
C1B
|
A:BPM403
|
4.8
|
21.8
|
0.5
|
C1B
|
A:BPM402
|
4.8
|
11.4
|
0.5
|
|
Reference:
Y.A.Puius,
Y.Zhao,
M.Sullivan,
D.S.Lawrence,
S.C.Almo,
Z.Y.Zhang.
Identification of A Second Aryl Phosphate-Binding Site in Protein-Tyrosine Phosphatase 1B: A Paradigm For Inhibitor Design. Proc.Natl.Acad.Sci.Usa V. 94 13420 1997.
ISSN: ISSN 0027-8424
PubMed: 9391040
DOI: 10.1073/PNAS.94.25.13420
Page generated: Fri Sep 25 12:41:49 2020
|