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Vanadium in PDB 7l0h: Vanadate-Bound PTP1B T177G

Enzymatic activity of Vanadate-Bound PTP1B T177G

All present enzymatic activity of Vanadate-Bound PTP1B T177G:
3.1.3.48;

Protein crystallography data

The structure of Vanadate-Bound PTP1B T177G, PDB code: 7l0h was solved by R.D.Shen, A.C.Hengge, S.J.Johnson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.30 / 2.10
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.471, 88.471, 104.979, 90, 90, 120
R / Rfree (%) 17.8 / 20.8

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Vanadate-Bound PTP1B T177G (pdb code 7l0h). 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 Vanadate-Bound PTP1B T177G, PDB code: 7l0h:

Vanadium binding site 1 out of 1 in 7l0h

Go back to Vanadium Binding Sites List in 7l0h
Vanadium binding site 1 out of 1 in the Vanadate-Bound PTP1B T177G


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Vanadate-Bound PTP1B T177G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V401

b:41.9
occ:1.00
V A:VO4401 0.0 41.9 1.0
O1 A:VO4401 1.9 35.7 1.0
O2 A:VO4401 1.9 40.9 1.0
O4 A:VO4401 1.9 42.0 1.0
O3 A:VO4401 2.0 36.5 1.0
SG A:CYS215 2.7 37.1 1.0
OD1 A:ASP181 3.6 47.8 1.0
OE1 A:GLN262 3.6 43.3 1.0
CB A:CYS215 3.7 34.6 1.0
N A:GLY220 3.8 41.1 1.0
N A:ALA217 3.8 37.8 1.0
O A:HOH548 3.9 40.3 1.0
NE A:ARG221 4.0 40.3 1.0
NH2 A:ARG221 4.0 41.2 1.0
N A:ARG221 4.1 36.9 1.0
CB A:ALA217 4.1 37.0 1.0
CA A:GLY220 4.1 39.0 1.0
N A:SER216 4.1 36.1 1.0
N A:GLY218 4.2 38.0 1.0
N A:ILE219 4.4 38.5 1.0
CA A:ALA217 4.4 36.4 1.0
CZ A:ARG221 4.5 43.9 1.0
CD A:GLN262 4.6 45.6 1.0
CG A:ASP181 4.6 46.0 1.0
C A:GLY220 4.7 43.2 1.0
C A:ALA217 4.8 37.8 1.0
O A:HOH624 4.8 47.3 1.0
C A:SER216 4.8 38.0 1.0
CA A:SER216 4.8 35.4 1.0
CB A:ARG221 4.8 38.2 1.0
CB A:SER216 4.9 40.1 1.0
CA A:CYS215 4.9 38.3 1.0
C A:ILE219 4.9 38.3 1.0
CG A:ARG221 4.9 36.3 1.0
C A:CYS215 4.9 36.2 1.0
OD2 A:ASP181 4.9 47.3 1.0
NE2 A:GLN262 5.0 41.9 1.0

Reference:

R.Shen, R.M.Crean, S.J.Johnson, S.C.L.Kamerlin, A.C.Hengge. Single Residue on the Wpd-Loop Affects the pH Dependency of Catalysis in Protein Tyrosine Phosphatases Jacs Au 2021.
DOI: 10.1021/JACSAU.1C00054
Page generated: Mon Jul 12 16:14:10 2021

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