Phosphorus in PDB 1a1c: C-Src (SH2 Domain) Complexed with Ace-Phosphotyr-Glu-(N-Me(-(CH2)3- Cyclopentyl))
Enzymatic activity of C-Src (SH2 Domain) Complexed with Ace-Phosphotyr-Glu-(N-Me(-(CH2)3- Cyclopentyl))
All present enzymatic activity of C-Src (SH2 Domain) Complexed with Ace-Phosphotyr-Glu-(N-Me(-(CH2)3- Cyclopentyl)):
2.7.1.112;
Protein crystallography data
The structure of C-Src (SH2 Domain) Complexed with Ace-Phosphotyr-Glu-(N-Me(-(CH2)3- Cyclopentyl)), PDB code: 1a1c
was solved by
L.Shewchuk,
S.Jordan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
6.00 /
2.40
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
51.700,
66.900,
75.600,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
18.6 /
n/a
|
Phosphorus Binding Sites:
The binding sites of Phosphorus atom in the C-Src (SH2 Domain) Complexed with Ace-Phosphotyr-Glu-(N-Me(-(CH2)3- Cyclopentyl))
(pdb code 1a1c). This binding sites where shown within
5.0 Angstroms radius around Phosphorus atom.
In total 2 binding sites of Phosphorus where determined in the
C-Src (SH2 Domain) Complexed with Ace-Phosphotyr-Glu-(N-Me(-(CH2)3- Cyclopentyl)), PDB code: 1a1c:
Jump to Phosphorus binding site number:
1;
2;
Phosphorus binding site 1 out
of 2 in 1a1c
Go back to
Phosphorus Binding Sites List in 1a1c
Phosphorus binding site 1 out
of 2 in the C-Src (SH2 Domain) Complexed with Ace-Phosphotyr-Glu-(N-Me(-(CH2)3- Cyclopentyl))
 Mono view
 Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 1 of C-Src (SH2 Domain) Complexed with Ace-Phosphotyr-Glu-(N-Me(-(CH2)3- Cyclopentyl)) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:P101
b:12.1
occ:1.00
|
P
|
C:PTR101
|
0.0
|
12.1
|
1.0
|
O1P
|
C:PTR101
|
1.4
|
17.0
|
1.0
|
O2P
|
C:PTR101
|
1.5
|
13.3
|
1.0
|
O3P
|
C:PTR101
|
1.5
|
14.7
|
1.0
|
OH
|
C:PTR101
|
1.8
|
9.7
|
1.0
|
CZ
|
C:PTR101
|
2.8
|
12.7
|
1.0
|
HH22
|
A:ARG178
|
2.9
|
0.0
|
1.0
|
HH12
|
A:ARG178
|
3.0
|
0.0
|
1.0
|
HE
|
A:ARG158
|
3.0
|
0.0
|
1.0
|
H
|
A:GLU181
|
3.3
|
0.0
|
1.0
|
HH21
|
A:ARG158
|
3.4
|
0.0
|
1.0
|
CE1
|
C:PTR101
|
3.5
|
14.6
|
1.0
|
H
|
A:THR182
|
3.5
|
0.0
|
1.0
|
CE2
|
C:PTR101
|
3.7
|
11.7
|
1.0
|
H1
|
C:HOH501
|
3.8
|
0.0
|
1.0
|
HG
|
A:SER180
|
3.8
|
0.0
|
1.0
|
O
|
C:HOH501
|
3.8
|
23.9
|
1.0
|
NH2
|
A:ARG178
|
3.8
|
12.6
|
1.0
|
NH1
|
A:ARG178
|
3.9
|
9.5
|
1.0
|
OG
|
A:SER180
|
3.9
|
17.7
|
1.0
|
NE
|
A:ARG158
|
4.0
|
20.7
|
1.0
|
HG1
|
A:THR182
|
4.1
|
0.0
|
1.0
|
N
|
A:GLU181
|
4.1
|
25.6
|
1.0
|
CB
|
A:THR182
|
4.2
|
25.6
|
1.0
|
NH2
|
A:ARG158
|
4.3
|
18.5
|
1.0
|
CZ
|
A:ARG178
|
4.3
|
15.2
|
1.0
|
OG1
|
A:THR182
|
4.4
|
28.2
|
1.0
|
CB
|
A:ARG158
|
4.4
|
13.3
|
1.0
|
N
|
A:THR182
|
4.4
|
29.7
|
1.0
|
CA
|
A:SER180
|
4.5
|
19.2
|
1.0
|
HH21
|
A:ARG178
|
4.6
|
0.0
|
1.0
|
HH11
|
A:ARG178
|
4.7
|
0.0
|
1.0
|
CZ
|
A:ARG158
|
4.7
|
15.7
|
1.0
|
CD1
|
C:PTR101
|
4.7
|
16.0
|
1.0
|
CG
|
A:ARG158
|
4.8
|
14.4
|
1.0
|
C
|
A:SER180
|
4.8
|
23.4
|
1.0
|
CB
|
A:SER180
|
4.8
|
15.9
|
1.0
|
H2
|
C:HOH501
|
4.8
|
0.0
|
1.0
|
CD
|
A:ARG158
|
4.8
|
16.1
|
1.0
|
CD2
|
C:PTR101
|
4.9
|
12.9
|
1.0
|
CB
|
A:GLU181
|
4.9
|
25.2
|
1.0
|
CG
|
A:GLU181
|
4.9
|
23.5
|
1.0
|
CG2
|
A:THR182
|
5.0
|
31.4
|
1.0
|
CA
|
A:GLU181
|
5.0
|
27.7
|
1.0
|
|
Phosphorus binding site 2 out
of 2 in 1a1c
Go back to
Phosphorus Binding Sites List in 1a1c
Phosphorus binding site 2 out
of 2 in the C-Src (SH2 Domain) Complexed with Ace-Phosphotyr-Glu-(N-Me(-(CH2)3- Cyclopentyl))
 Mono view
 Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 2 of C-Src (SH2 Domain) Complexed with Ace-Phosphotyr-Glu-(N-Me(-(CH2)3- Cyclopentyl)) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:P101
b:34.6
occ:1.00
|
P
|
D:PTR101
|
0.0
|
34.6
|
1.0
|
O1P
|
D:PTR101
|
1.5
|
36.4
|
1.0
|
O2P
|
D:PTR101
|
1.5
|
32.3
|
1.0
|
O3P
|
D:PTR101
|
1.5
|
39.4
|
1.0
|
OH
|
D:PTR101
|
1.7
|
30.0
|
1.0
|
CZ
|
D:PTR101
|
2.6
|
29.4
|
1.0
|
HH12
|
B:ARG178
|
2.8
|
0.0
|
1.0
|
HH22
|
B:ARG178
|
2.8
|
0.0
|
1.0
|
H
|
B:GLU181
|
3.1
|
0.0
|
1.0
|
HE
|
B:ARG158
|
3.4
|
0.0
|
1.0
|
H
|
B:THR182
|
3.4
|
0.0
|
1.0
|
CE1
|
D:PTR101
|
3.4
|
24.1
|
1.0
|
HG1
|
B:THR182
|
3.5
|
0.0
|
1.0
|
CE2
|
D:PTR101
|
3.5
|
26.4
|
1.0
|
HH21
|
B:ARG158
|
3.6
|
0.0
|
1.0
|
NH1
|
B:ARG178
|
3.7
|
16.0
|
1.0
|
NH2
|
B:ARG178
|
3.7
|
15.4
|
1.0
|
OG
|
B:SER180
|
3.7
|
32.1
|
1.0
|
OG1
|
B:THR182
|
4.0
|
49.6
|
1.0
|
N
|
B:GLU181
|
4.0
|
40.8
|
1.0
|
CZ
|
B:ARG178
|
4.2
|
18.1
|
1.0
|
CB
|
B:THR182
|
4.3
|
48.1
|
1.0
|
HG
|
B:SER180
|
4.3
|
0.0
|
1.0
|
NE
|
B:ARG158
|
4.3
|
39.3
|
1.0
|
N
|
B:THR182
|
4.4
|
49.1
|
1.0
|
CA
|
B:SER180
|
4.4
|
32.9
|
1.0
|
HH11
|
B:ARG178
|
4.5
|
0.0
|
1.0
|
HH21
|
B:ARG178
|
4.5
|
0.0
|
1.0
|
NH2
|
B:ARG158
|
4.5
|
47.6
|
1.0
|
CB
|
B:ARG158
|
4.6
|
24.1
|
1.0
|
CB
|
B:GLU181
|
4.6
|
47.1
|
1.0
|
OE2
|
B:GLU181
|
4.6
|
52.7
|
1.0
|
CD1
|
D:PTR101
|
4.7
|
26.7
|
1.0
|
C
|
B:SER180
|
4.7
|
36.7
|
1.0
|
CD2
|
D:PTR101
|
4.7
|
28.7
|
1.0
|
CB
|
B:SER180
|
4.7
|
28.7
|
1.0
|
CG
|
B:GLU181
|
4.8
|
51.6
|
1.0
|
CA
|
B:GLU181
|
4.9
|
45.1
|
1.0
|
CZ
|
B:ARG158
|
5.0
|
43.4
|
1.0
|
|
Reference:
P.S.Charifson,
L.M.Shewchuk,
W.Rocque,
C.W.Hummel,
S.R.Jordan,
C.Mohr,
G.J.Pacofsky,
M.R.Peel,
M.Rodriguez,
D.D.Sternbach,
T.G.Consler.
Peptide Ligands of PP60(C-Src) SH2 Domains: A Thermodynamic and Structural Study. Biochemistry V. 36 6283 1997.
ISSN: ISSN 0006-2960
PubMed: 9174343
DOI: 10.1021/BI970019N
Page generated: Fri Sep 25 11:57:25 2020
|