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Vanadium in PDB 6xea: Crystal Structure of the PTP1B Yoph Wpd Loop Chimera 3 Bound to Vanadate

Enzymatic activity of Crystal Structure of the PTP1B Yoph Wpd Loop Chimera 3 Bound to Vanadate

All present enzymatic activity of Crystal Structure of the PTP1B Yoph Wpd Loop Chimera 3 Bound to Vanadate:
3.1.3.48;

Protein crystallography data

The structure of Crystal Structure of the PTP1B Yoph Wpd Loop Chimera 3 Bound to Vanadate, PDB code: 6xea was solved by K.J.Olsen, R.Shen, 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) 44.29 / 1.55
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.586, 88.586, 104.658, 90, 90, 120
R / Rfree (%) 18.7 / 19.9

Other elements in 6xea:

The structure of Crystal Structure of the PTP1B Yoph Wpd Loop Chimera 3 Bound to Vanadate also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Crystal Structure of the PTP1B Yoph Wpd Loop Chimera 3 Bound to Vanadate (pdb code 6xea). 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 Crystal Structure of the PTP1B Yoph Wpd Loop Chimera 3 Bound to Vanadate, PDB code: 6xea:

Vanadium binding site 1 out of 1 in 6xea

Go back to Vanadium Binding Sites List in 6xea
Vanadium binding site 1 out of 1 in the Crystal Structure of the PTP1B Yoph Wpd Loop Chimera 3 Bound to Vanadate


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 the PTP1B Yoph Wpd Loop Chimera 3 Bound to Vanadate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V401

b:25.7
occ:0.84
 V A:VO4401 0.0 25.7 0.8
O1 A:VO4401 1.8 20.7 0.8
O3 A:VO4401 1.8 29.6 0.8
O2 A:VO4401 1.8 21.0 0.8
O4 A:VO4401 1.8 20.5 0.8
SG A:CYS215 2.6 20.0 1.0
CB A:CYS215 3.5 20.4 1.0
OD1 A:ASP181 3.7 41.4 1.0
OE1 A:GLN262 3.7 30.8 0.4
N A:GLY220 3.7 21.5 1.0
N A:ALA217 3.9 20.7 1.0
O A:HOH511 4.0 29.6 1.0
N A:ARG221 4.0 22.0 1.0
NE A:ARG221 4.0 22.2 1.0
NH2 A:ARG221 4.0 22.4 1.0
N A:SER216 4.1 19.1 1.0
CA A:GLY220 4.2 21.5 1.0
N A:GLY218 4.2 19.4 1.0
CB A:ALA217 4.3 23.4 1.0
N A:ILE219 4.4 20.6 1.0
CZ A:ARG221 4.5 20.5 1.0
CG A:ASP181 4.5 45.6 1.0
CA A:ALA217 4.5 20.8 1.0
C A:GLY220 4.6 22.5 1.0
CA A:CYS215 4.7 20.2 1.0
CD A:GLN262 4.7 28.8 0.4
CB A:ARG221 4.8 20.2 1.0
OD2 A:ASP181 4.8 51.2 1.0
C A:CYS215 4.8 18.4 1.0
C A:ALA217 4.8 21.8 1.0
C A:SER216 4.9 19.4 1.0
CA A:SER216 4.9 18.7 1.0
C A:ILE219 4.9 23.6 1.0
CG A:ARG221 5.0 21.6 1.0
CA A:ARG221 5.0 20.9 1.0

Reference:

K.J.Olsen, R.Shen, S.J.Johnson, A.C.Hengge. Insights From PTP1B Yoph Chimeras Into the Importance of Wpd-Loop Sequence For Activity and Structure in Protein Tyrosine Phosphatases To Be Published.
Page generated: Fri Dec 17 11:26:07 2021

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