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Vanadium in PDB 3qkq: Protein Tyrosine Phosphatase 1B - W179F Mutant Bound with Vanadate

Enzymatic activity of Protein Tyrosine Phosphatase 1B - W179F Mutant Bound with Vanadate

All present enzymatic activity of Protein Tyrosine Phosphatase 1B - W179F Mutant Bound with Vanadate:
3.1.3.48;

Protein crystallography data

The structure of Protein Tyrosine Phosphatase 1B - W179F Mutant Bound with Vanadate, PDB code: 3qkq was solved by T.A.S.Brandao, S.J.Johnson, A.C.Hengge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.37 / 2.20
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.620, 88.620, 104.320, 90.00, 90.00, 120.00
R / Rfree (%) 19.6 / 25.4

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Protein Tyrosine Phosphatase 1B - W179F Mutant Bound with Vanadate (pdb code 3qkq). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total only one binding site of Vanadium was determined in the Protein Tyrosine Phosphatase 1B - W179F Mutant Bound with Vanadate, PDB code: 3qkq:

Vanadium binding site 1 out of 1 in 3qkq

Go back to Vanadium Binding Sites List in 3qkq
Vanadium binding site 1 out of 1 in the Protein Tyrosine Phosphatase 1B - W179F Mutant Bound with Vanadate


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Protein Tyrosine Phosphatase 1B - W179F Mutant Bound with Vanadate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V322

b:79.7
occ:1.00
V A:VO4322 0.0 79.7 1.0
O1 A:VO4322 1.9 76.7 1.0
O3 A:VO4322 1.9 78.2 1.0
O2 A:VO4322 1.9 77.5 1.0
O4 A:VO4322 2.1 80.6 1.0
SG A:CYS215 2.6 36.3 1.0
CB A:CYS215 3.6 27.5 1.0
OE1 A:GLN262 3.6 49.5 1.0
N A:GLY220 3.8 31.4 1.0
N A:ALA217 3.8 33.5 1.0
O A:HOH341 3.8 48.8 1.0
N A:SER216 4.0 27.5 1.0
NH2 A:ARG221 4.1 32.8 0.5
CB A:ALA217 4.1 37.3 1.0
OD1 A:ASP181 4.1 35.6 0.5
NE A:ARG221 4.2 34.7 0.5
CA A:GLY220 4.2 28.3 1.0
N A:ARG221 4.2 21.8 1.0
N A:GLY218 4.2 34.5 1.0
O1 A:GOL326 4.2 80.4 1.0
N A:ILE219 4.3 33.3 1.0
CA A:ALA217 4.4 34.6 1.0
CZ A:ARG221 4.6 36.6 0.5
CD A:GLN262 4.6 48.9 1.0
CA A:CYS215 4.7 27.8 1.0
C A:SER216 4.7 29.6 1.0
C A:GLY220 4.8 30.5 1.0
C A:ALA217 4.8 36.9 1.0
CA A:SER216 4.8 33.8 1.0
C A:CYS215 4.8 28.6 1.0
C A:ILE219 4.9 31.2 1.0
CG1 A:ILE219 4.9 34.0 1.0
CB A:SER216 4.9 35.7 1.0
CG A:ASP181 4.9 40.0 0.5
CG A:ARG221 5.0 29.2 0.5

Reference:

T.A.Brandao, S.J.Johnson, A.C.Hengge. The Molecular Details of Wpd-Loop Movement Differ in the Protein-Tyrosine Phosphatases Yoph and PTP1B. Arch.Biochem.Biophys. V. 525 53 2012.
ISSN: ISSN 0003-9861
PubMed: 22698963
DOI: 10.1016/J.ABB.2012.06.002
Page generated: Thu Oct 29 07:05:14 2020

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