Vanadium in PDB 5z5a: Crystal Structure of Tk-Ptp in the Active Form
Protein crystallography data
The structure of Crystal Structure of Tk-Ptp in the Active Form, PDB code: 5z5a
was solved by
B.Ku,
H.Y.Yun,
S.J.Kim,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
27.96 /
1.80
|
Space group
|
P 61
|
Cell size a, b, c (Å), α, β, γ (°)
|
102.722,
102.722,
83.805,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
17.4 /
20.9
|
Vanadium Binding Sites:
The binding sites of Vanadium atom in the Crystal Structure of Tk-Ptp in the Active Form
(pdb code 5z5a). This binding sites where shown within
5.0 Angstroms radius around Vanadium atom.
In total 3 binding sites of Vanadium where determined in the
Crystal Structure of Tk-Ptp in the Active Form, PDB code: 5z5a:
Jump to Vanadium binding site number:
1;
2;
3;
Vanadium binding site 1 out
of 3 in 5z5a
Go back to
Vanadium Binding Sites List in 5z5a
Vanadium binding site 1 out
of 3 in the Crystal Structure of Tk-Ptp in the Active Form
Mono view
Stereo pair view
|
A full contact list of Vanadium with other atoms in the V binding
site number 1 of Crystal Structure of Tk-Ptp in the Active Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:V201
b:22.0
occ:1.00
|
V
|
A:VN3201
|
0.0
|
22.0
|
1.0
|
O1
|
A:VN3201
|
1.9
|
18.1
|
1.0
|
O2
|
A:VN3201
|
1.9
|
14.8
|
1.0
|
O3
|
A:VN3201
|
1.9
|
17.8
|
1.0
|
SG
|
A:CYS93
|
2.6
|
13.4
|
1.0
|
CB
|
A:CYS93
|
3.5
|
13.7
|
1.0
|
N
|
A:GLY95
|
3.6
|
14.9
|
1.0
|
N
|
A:GLY98
|
3.7
|
15.2
|
1.0
|
NE
|
A:ARG99
|
3.8
|
16.5
|
1.0
|
N
|
A:MET94
|
3.8
|
12.5
|
1.0
|
NH2
|
A:ARG99
|
3.9
|
13.5
|
1.0
|
N
|
A:ARG99
|
3.9
|
14.0
|
1.0
|
O
|
A:HOH308
|
4.0
|
18.2
|
1.0
|
OD1
|
A:ASP63
|
4.0
|
16.4
|
1.0
|
N
|
A:LEU97
|
4.1
|
13.3
|
1.0
|
N
|
A:GLY96
|
4.1
|
12.5
|
1.0
|
OE1
|
A:GLU132
|
4.2
|
21.7
|
1.0
|
CA
|
A:GLY95
|
4.2
|
13.2
|
1.0
|
CZ
|
A:ARG99
|
4.3
|
16.4
|
1.0
|
CA
|
A:GLY98
|
4.4
|
14.4
|
1.0
|
CB
|
A:ARG99
|
4.5
|
14.6
|
1.0
|
C
|
A:MET94
|
4.5
|
12.4
|
1.0
|
C
|
A:GLY95
|
4.6
|
15.3
|
1.0
|
CA
|
A:MET94
|
4.6
|
14.7
|
1.0
|
C
|
A:LEU97
|
4.6
|
14.6
|
1.0
|
C
|
A:GLY98
|
4.6
|
14.1
|
1.0
|
C
|
A:CYS93
|
4.7
|
14.6
|
1.0
|
CA
|
A:CYS93
|
4.7
|
15.9
|
1.0
|
CA
|
A:LEU97
|
4.7
|
16.8
|
1.0
|
CB
|
A:MET94
|
4.8
|
16.0
|
1.0
|
CG
|
A:ARG99
|
4.8
|
18.6
|
1.0
|
CA
|
A:ARG99
|
4.8
|
14.1
|
1.0
|
CD
|
A:ARG99
|
4.9
|
15.7
|
1.0
|
CG
|
A:ASP63
|
4.9
|
17.6
|
1.0
|
CD
|
A:GLU132
|
5.0
|
22.8
|
1.0
|
CB
|
A:LEU97
|
5.0
|
17.1
|
1.0
|
CA
|
A:GLY96
|
5.0
|
11.8
|
1.0
|
C
|
A:GLY96
|
5.0
|
15.7
|
1.0
|
|
Vanadium binding site 2 out
of 3 in 5z5a
Go back to
Vanadium Binding Sites List in 5z5a
Vanadium binding site 2 out
of 3 in the Crystal Structure of Tk-Ptp in the Active Form
Mono view
Stereo pair view
|
A full contact list of Vanadium with other atoms in the V binding
site number 2 of Crystal Structure of Tk-Ptp in the Active Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:V201
b:26.4
occ:1.00
|
V
|
B:VN3201
|
0.0
|
26.4
|
1.0
|
O1
|
B:VN3201
|
1.9
|
18.6
|
1.0
|
O3
|
B:VN3201
|
1.9
|
19.9
|
1.0
|
O2
|
B:VN3201
|
1.9
|
17.8
|
1.0
|
SG
|
B:CYS93
|
2.7
|
17.2
|
1.0
|
CB
|
B:CYS93
|
3.5
|
15.9
|
1.0
|
N
|
B:GLY95
|
3.6
|
20.1
|
1.0
|
N
|
B:GLY98
|
3.7
|
16.7
|
1.0
|
N
|
B:ARG99
|
3.8
|
12.0
|
1.0
|
NE
|
B:ARG99
|
3.8
|
14.2
|
1.0
|
OD1
|
B:ASP63
|
3.8
|
14.5
|
1.0
|
N
|
B:MET94
|
3.9
|
15.5
|
1.0
|
O
|
B:HOH303
|
3.9
|
14.6
|
1.0
|
NH2
|
B:ARG99
|
3.9
|
14.1
|
1.0
|
N
|
B:GLY96
|
4.0
|
16.7
|
1.0
|
OE1
|
B:GLU132
|
4.1
|
17.9
|
1.0
|
N
|
B:LEU97
|
4.1
|
17.1
|
1.0
|
CA
|
B:GLY95
|
4.2
|
16.3
|
1.0
|
CA
|
B:GLY98
|
4.3
|
14.1
|
1.0
|
CZ
|
B:ARG99
|
4.4
|
16.0
|
1.0
|
CB
|
B:ARG99
|
4.5
|
15.5
|
1.0
|
C
|
B:GLY95
|
4.5
|
23.4
|
1.0
|
C
|
B:MET94
|
4.5
|
17.8
|
1.0
|
C
|
B:GLY98
|
4.6
|
14.3
|
1.0
|
CA
|
B:MET94
|
4.6
|
16.0
|
1.0
|
C
|
B:LEU97
|
4.6
|
18.8
|
1.0
|
C
|
B:CYS93
|
4.7
|
15.3
|
1.0
|
CA
|
B:CYS93
|
4.7
|
16.4
|
1.0
|
CG
|
B:ASP63
|
4.7
|
15.9
|
1.0
|
CA
|
B:ARG99
|
4.8
|
13.7
|
1.0
|
CB
|
B:MET94
|
4.8
|
18.3
|
1.0
|
CG
|
B:ARG99
|
4.8
|
14.8
|
1.0
|
CA
|
B:LEU97
|
4.8
|
16.1
|
1.0
|
CD
|
B:ARG99
|
4.9
|
12.4
|
1.0
|
CD
|
B:GLU132
|
4.9
|
19.8
|
1.0
|
CA
|
B:GLY96
|
4.9
|
16.6
|
1.0
|
OD2
|
B:ASP63
|
5.0
|
16.1
|
1.0
|
|
Vanadium binding site 3 out
of 3 in 5z5a
Go back to
Vanadium Binding Sites List in 5z5a
Vanadium binding site 3 out
of 3 in the Crystal Structure of Tk-Ptp in the Active Form
Mono view
Stereo pair view
|
A full contact list of Vanadium with other atoms in the V binding
site number 3 of Crystal Structure of Tk-Ptp in the Active Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:V201
b:24.1
occ:1.00
|
V
|
C:VN3201
|
0.0
|
24.1
|
1.0
|
O1
|
C:VN3201
|
1.9
|
20.1
|
1.0
|
O2
|
C:VN3201
|
1.9
|
19.7
|
1.0
|
O3
|
C:VN3201
|
1.9
|
22.3
|
1.0
|
SG
|
C:CYS93
|
2.6
|
19.8
|
1.0
|
CB
|
C:CYS93
|
3.5
|
24.0
|
1.0
|
N
|
C:GLY95
|
3.6
|
20.7
|
1.0
|
N
|
C:GLY98
|
3.7
|
20.4
|
1.0
|
NH2
|
C:ARG99
|
3.8
|
20.1
|
1.0
|
NE
|
C:ARG99
|
3.8
|
17.1
|
1.0
|
N
|
C:ARG99
|
3.8
|
19.5
|
1.0
|
N
|
C:MET94
|
3.9
|
19.2
|
1.0
|
OD1
|
C:ASP63
|
3.9
|
18.6
|
1.0
|
N
|
C:GLY96
|
4.0
|
17.3
|
1.0
|
OE1
|
C:GLU132
|
4.0
|
19.6
|
1.0
|
N
|
C:LEU97
|
4.1
|
16.1
|
1.0
|
O
|
C:HOH319
|
4.1
|
15.8
|
1.0
|
CA
|
C:GLY95
|
4.2
|
21.1
|
1.0
|
CZ
|
C:ARG99
|
4.3
|
22.0
|
1.0
|
CA
|
C:GLY98
|
4.3
|
16.2
|
1.0
|
C
|
C:GLY95
|
4.5
|
19.8
|
1.0
|
C
|
C:GLY98
|
4.5
|
19.6
|
1.0
|
CB
|
C:ARG99
|
4.6
|
17.3
|
1.0
|
C
|
C:MET94
|
4.6
|
24.2
|
1.0
|
C
|
C:LEU97
|
4.6
|
22.1
|
1.0
|
CA
|
C:MET94
|
4.6
|
20.5
|
1.0
|
CA
|
C:CYS93
|
4.7
|
21.6
|
1.0
|
C
|
C:CYS93
|
4.7
|
24.5
|
1.0
|
CA
|
C:LEU97
|
4.7
|
20.6
|
1.0
|
CA
|
C:ARG99
|
4.8
|
20.0
|
1.0
|
CB
|
C:MET94
|
4.8
|
21.2
|
1.0
|
CD
|
C:GLU132
|
4.8
|
17.4
|
1.0
|
CG
|
C:ASP63
|
4.9
|
18.2
|
1.0
|
CA
|
C:GLY96
|
4.9
|
21.0
|
1.0
|
CG
|
C:ARG99
|
4.9
|
20.1
|
1.0
|
CD
|
C:ARG99
|
4.9
|
16.5
|
1.0
|
CB
|
C:LEU97
|
5.0
|
17.3
|
1.0
|
C
|
C:GLY96
|
5.0
|
21.6
|
1.0
|
|
Reference:
H.Y.Yun,
J.Lee,
H.Kim,
H.Ryu,
H.C.Shin,
B.H.Oh,
B.Ku,
S.J.Kim.
Structural Study Reveals the Temperature-Dependent Conformational Flexibility of Tk-Ptp, A Protein Tyrosine Phosphatase From Thermococcus Kodakaraensis KOD1 Plos One V. 13 97635 2018.
ISSN: ESSN 1932-6203
PubMed: 29791483
DOI: 10.1371/JOURNAL.PONE.0197635
Page generated: Fri Oct 11 20:01:45 2024
|