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Vanadium in PDB 4ri5: Crystal Structure of PTPN3 (PTPH1) D811E Mutant in Complex with Metavanadate

Enzymatic activity of Crystal Structure of PTPN3 (PTPH1) D811E Mutant in Complex with Metavanadate

All present enzymatic activity of Crystal Structure of PTPN3 (PTPH1) D811E Mutant in Complex with Metavanadate:
3.1.3.48;

Protein crystallography data

The structure of Crystal Structure of PTPN3 (PTPH1) D811E Mutant in Complex with Metavanadate, PDB code: 4ri5 was solved by K.-E.Chen, T.C.Meng, A.H.-J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.54 / 1.26
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 95.162, 96.071, 141.722, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 17.3

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Crystal Structure of PTPN3 (PTPH1) D811E Mutant in Complex with Metavanadate (pdb code 4ri5). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the Crystal Structure of PTPN3 (PTPH1) D811E Mutant in Complex with Metavanadate, PDB code: 4ri5:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in 4ri5

Go back to Vanadium Binding Sites List in 4ri5
Vanadium binding site 1 out of 2 in the Crystal Structure of PTPN3 (PTPH1) D811E Mutant in Complex with Metavanadate


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 PTPN3 (PTPH1) D811E Mutant in Complex with Metavanadate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V1002

b:14.9
occ:0.72
V A:VN41002 0.0 14.9 0.7
O1 A:VN41002 1.7 15.5 1.0
O2 A:VN41002 1.7 15.2 1.0
O3 A:VN41002 1.7 14.7 1.0
SG A:CYS842 2.3 14.8 1.0
H A:GLY847 2.9 13.3 1.0
H A:ALA844 3.0 14.9 1.0
HH21 A:ARG848 3.0 17.8 1.0
HE A:ARG848 3.0 15.6 1.0
HB2 A:CYS842 3.0 16.1 1.0
H A:ARG848 3.2 14.3 1.0
H A:SER843 3.2 16.4 1.0
H A:GLY845 3.3 16.0 1.0
H A:ILE846 3.3 13.7 1.0
CB A:CYS842 3.3 13.5 1.0
HB3 A:ALA844 3.5 16.2 1.0
O A:HOH1384 3.6 18.7 1.0
N A:GLY847 3.7 11.1 1.0
N A:ALA844 3.8 12.4 1.0
NH2 A:ARG848 3.8 14.9 1.0
O A:HOH1176 3.8 20.2 1.0
NE A:ARG848 3.8 13.0 1.0
HB2 A:ARG848 3.9 14.3 1.0
HB3 A:CYS842 3.9 16.1 1.0
N A:SER843 3.9 13.6 1.0
N A:GLY845 3.9 13.3 1.0
N A:ARG848 4.0 11.9 1.0
HA3 A:GLY847 4.0 14.7 1.0
N A:ILE846 4.1 11.4 1.0
OE1 A:GLN886 4.1 13.7 0.6
HB3 A:SER843 4.2 15.9 1.0
CA A:GLY847 4.3 12.2 1.0
CB A:ALA844 4.3 13.5 1.0
HG3 A:ARG848 4.3 14.0 1.0
CZ A:ARG848 4.3 13.8 1.0
H A:THR849 4.3 13.8 0.4
H A:THR849 4.4 13.8 0.6
HO1 A:GOL1001 4.4 16.8 0.6
CA A:ALA844 4.4 13.4 1.0
HG13 A:ILE846 4.4 16.5 1.0
CA A:CYS842 4.5 14.1 1.0
HG3 A:GLU811 4.5 23.4 1.0
HH22 A:ARG848 4.5 17.8 1.0
C A:ALA844 4.6 13.0 1.0
C A:CYS842 4.6 12.8 1.0
CB A:ARG848 4.6 11.9 1.0
HG1 A:THR849 4.7 18.6 0.4
HB2 A:ALA844 4.7 16.2 1.0
C A:GLY847 4.7 10.6 1.0
HG12 A:ILE846 4.7 16.5 1.0
CA A:SER843 4.7 12.9 1.0
C A:ILE846 4.7 11.9 1.0
C A:SER843 4.7 12.4 1.0
HA2 A:GLY845 4.7 15.3 1.0
CA A:GLY845 4.7 12.7 1.0
HG23 A:THR849 4.8 17.6 0.6
CG A:ARG848 4.8 11.6 1.0
H A:CYS842 4.9 15.4 1.0
C A:GLY845 4.9 12.0 1.0
CB A:SER843 4.9 13.3 1.0
CA A:ARG848 4.9 11.6 1.0
CA A:ILE846 4.9 11.8 1.0
CD A:ARG848 4.9 12.9 1.0
CD A:GLN886 4.9 19.3 1.0

Vanadium binding site 2 out of 2 in 4ri5

Go back to Vanadium Binding Sites List in 4ri5
Vanadium binding site 2 out of 2 in the Crystal Structure of PTPN3 (PTPH1) D811E Mutant in Complex with Metavanadate


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 PTPN3 (PTPH1) D811E Mutant in Complex with Metavanadate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:V1002

b:14.6
occ:0.87
V B:VN41002 0.0 14.6 0.9
O1 B:VN41002 1.7 13.6 1.0
O2 B:VN41002 1.7 13.3 1.0
O3 B:VN41002 1.7 13.8 1.0
SG B:CYS842 2.3 13.7 1.0
H B:GLY847 2.9 13.5 1.0
H B:ALA844 3.0 15.0 1.0
HE B:ARG848 3.0 14.5 1.0
HH21 B:ARG848 3.1 16.8 1.0
HB2 B:CYS842 3.1 15.6 1.0
H B:ARG848 3.2 13.6 1.0
H B:SER843 3.2 14.7 1.0
H B:GLY845 3.2 14.3 1.0
H B:ILE846 3.3 13.7 1.0
CB B:CYS842 3.3 13.0 1.0
HB3 B:ALA844 3.5 14.9 1.0
N B:GLY847 3.7 11.3 1.0
O B:HOH1122 3.8 15.9 1.0
N B:ALA844 3.8 12.5 1.0
NE B:ARG848 3.8 12.1 1.0
NH2 B:ARG848 3.9 14.0 1.0
O B:HOH1415 3.9 18.5 1.0
HB3 B:CYS842 3.9 15.6 1.0
HB2 B:ARG848 3.9 14.3 1.0
N B:GLY845 3.9 11.9 1.0
N B:SER843 3.9 12.2 1.0
HA3 B:GLY847 3.9 13.7 1.0
N B:ARG848 4.0 11.3 1.0
N B:ILE846 4.1 11.4 1.0
OE1 B:GLN886 4.1 17.8 1.0
HB3 B:SER843 4.2 14.8 1.0
CA B:GLY847 4.3 11.4 1.0
HG3 B:ARG848 4.3 13.5 1.0
CB B:ALA844 4.3 12.4 1.0
CZ B:ARG848 4.3 12.4 1.0
HG13 B:ILE846 4.4 14.6 1.0
HO1 B:GOL1001 4.4 21.0 1.0
H B:THR849 4.4 13.7 0.4
H B:THR849 4.4 13.7 0.6
CA B:ALA844 4.4 13.0 1.0
CA B:CYS842 4.5 12.3 1.0
HG3 B:GLU811 4.5 22.6 1.0
HH22 B:ARG848 4.5 16.8 1.0
C B:ALA844 4.6 13.6 1.0
HB2 B:ALA844 4.6 14.9 1.0
CB B:ARG848 4.6 11.9 1.0
C B:CYS842 4.7 12.5 1.0
C B:ILE846 4.7 11.4 1.0
C B:GLY847 4.7 11.2 1.0
HA2 B:GLY845 4.7 15.5 1.0
HG12 B:ILE846 4.7 14.6 1.0
CA B:GLY845 4.7 12.9 1.0
C B:SER843 4.7 11.7 1.0
CA B:SER843 4.7 12.3 1.0
HG1 B:THR849 4.8 18.8 0.4
CG B:ARG848 4.8 11.3 1.0
C B:GLY845 4.9 12.1 1.0
H B:CYS842 4.9 15.2 1.0
CA B:ILE846 4.9 11.5 1.0
CA B:ARG848 4.9 11.2 1.0
CB B:SER843 4.9 12.3 1.0
CD B:ARG848 4.9 12.3 1.0
HG1 B:THR849 4.9 12.5 0.6
HG23 B:THR849 5.0 16.6 0.6
CD B:GLN886 5.0 15.6 1.0
CG1 B:ILE846 5.0 12.2 1.0
HB1 B:ALA844 5.0 14.9 1.0

Reference:

K.E.Chen, M.Y.Li, C.C.Chou, M.R.Ho, G.C.Chen, T.C.Meng, A.H.Wang. Substrate Specificity and Plasticity of Ferm-Containing Protein Tyrosine Phosphatases. Structure 2015.
ISSN: ISSN 0969-2126
PubMed: 25728925
DOI: 10.1016/J.STR.2015.01.017
Page generated: Wed Dec 16 02:31:19 2020

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