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Vanadium in PDB 3i7z: Protein Tyrosine Phosphatase 1B - Transition State Analog For the First Catalytic Step

Enzymatic activity of Protein Tyrosine Phosphatase 1B - Transition State Analog For the First Catalytic Step

All present enzymatic activity of Protein Tyrosine Phosphatase 1B - Transition State Analog For the First Catalytic Step:
3.1.3.48;

Protein crystallography data

The structure of Protein Tyrosine Phosphatase 1B - Transition State Analog For the First Catalytic Step, PDB code: 3i7z 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) 27.64 / 2.30
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.020, 88.020, 118.620, 90.00, 90.00, 120.00
R / Rfree (%) 20.6 / 23.3

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Protein Tyrosine Phosphatase 1B - Transition State Analog For the First Catalytic Step (pdb code 3i7z). 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 - Transition State Analog For the First Catalytic Step, PDB code: 3i7z:

Vanadium binding site 1 out of 1 in 3i7z

Go back to Vanadium Binding Sites List in 3i7z
Vanadium binding site 1 out of 1 in the Protein Tyrosine Phosphatase 1B - Transition State Analog For the First Catalytic Step


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 - Transition State Analog For the First Catalytic Step within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V322

b:56.0
occ:1.00
V A:VO4322 0.0 56.0 1.0
O2 A:VO4322 1.9 54.0 1.0
O3 A:VO4322 1.9 58.8 1.0
O1 A:VO4322 1.9 56.8 1.0
OH B:TYR992 2.1 59.9 1.0
SG A:CYS215 2.5 56.0 1.0
CZ B:TYR992 3.1 65.6 1.0
CB A:CYS215 3.5 57.7 1.0
O A:HOH465 3.7 70.9 1.0
N A:GLY220 3.8 47.4 1.0
OD1 A:ASP181 3.8 55.5 1.0
CE1 B:TYR992 3.8 63.2 1.0
N A:ALA217 3.9 54.5 1.0
NH2 A:ARG221 3.9 52.0 1.0
NE A:ARG221 3.9 58.3 1.0
N A:SER216 4.1 50.8 1.0
N A:ARG221 4.1 49.4 1.0
N A:GLY218 4.1 54.9 1.0
CE2 B:TYR992 4.1 64.3 1.0
CA A:GLY220 4.2 45.6 1.0
CB A:ALA217 4.3 59.5 1.0
N A:ILE219 4.4 51.4 1.0
CZ A:ARG221 4.4 57.0 1.0
CA A:ALA217 4.5 50.9 1.0
CG A:ASP181 4.7 56.6 1.0
C A:GLY220 4.7 56.7 1.0
CA A:CYS215 4.7 44.8 1.0
C A:ALA217 4.7 51.2 1.0
C A:CYS215 4.7 47.4 1.0
CG1 A:ILE219 4.8 52.2 1.0
CA A:SER216 4.8 48.5 1.0
C A:SER216 4.8 50.6 1.0
C A:ILE219 4.9 53.3 1.0
OD2 A:ASP181 4.9 52.7 1.0
CB A:ARG221 4.9 54.8 1.0
CG A:ARG221 4.9 55.1 1.0
CA A:GLY218 4.9 53.8 1.0
CB A:SER216 5.0 54.6 1.0

Reference:

T.A.Brandao, A.C.Hengge, S.J.Johnson. Insights Into the Reaction of Protein-Tyrosine Phosphatase 1B: Crystal Structures For Transition State Analogs of Both Catalytic Steps. J.Biol.Chem. V. 285 15874 2010.
ISSN: ISSN 0021-9258
PubMed: 20236928
DOI: 10.1074/JBC.M109.066951
Page generated: Wed Dec 16 02:30:51 2020

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