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Vanadium in PDB 5a3q: Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp

Enzymatic activity of Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp

All present enzymatic activity of Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp:
3.6.3.8;

Protein crystallography data

The structure of Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp, PDB code: 5a3q was solved by J.D.Clausen, M.Bublitz, B.Arnou, C.Olesen, J.P.Andersen, J.V.Moller, P.Nissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 73.80 / 3.05
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.427, 118.781, 141.828, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 25.8

Other elements in 5a3q:

The structure of Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Potassium (K) 1 atom
Chlorine (Cl) 1 atom

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp (pdb code 5a3q). 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 (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp, PDB code: 5a3q:

Vanadium binding site 1 out of 1 in 5a3q

Go back to Vanadium Binding Sites List in 5a3q
Vanadium binding site 1 out of 1 in the Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp


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 (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V1001

b:57.7
occ:1.00
 V A:VN41001 0.0 57.7 1.0
O2 A:VN41001 1.6 73.8 1.0
O3 A:VN41001 1.7 52.7 1.0
O1 A:VN41001 1.7 63.0 1.0
OD1 A:ASP351 2.0 61.4 1.0
O A:HOH2001 2.1 89.0 1.0
CG A:ASP351 3.0 53.9 1.0
OD2 A:ASP351 3.3 54.4 1.0
O A:HOH2003 3.6 42.3 1.0
MG A:MG1003 3.6 36.6 1.0
N A:THR353 3.9 56.1 1.0
OG1 A:THR625 4.0 54.3 1.0
N A:LYS352 4.0 52.4 1.0
O A:THR181 4.0 62.4 1.0
N A:GLY626 4.1 57.2 1.0
NZ A:LYS684 4.1 49.9 1.0
O A:GLY182 4.1 59.1 1.0
CB A:THR353 4.1 56.4 1.0
O A:THR353 4.2 64.7 1.0
CA A:GLY182 4.2 58.0 1.0
ND2 A:ASN706 4.3 46.8 1.0
CB A:ASP351 4.3 56.8 1.0
CA A:THR625 4.3 54.3 1.0
C A:GLY182 4.4 50.6 1.0
OE2 A:GLU183 4.4 67.2 1.0
CA A:THR353 4.5 54.0 1.0
CB A:THR625 4.5 41.5 1.0
C A:LYS352 4.6 50.8 1.0
OG1 A:THR353 4.6 67.1 1.0
O A:HOH2002 4.7 42.1 1.0
CA A:LYS352 4.7 46.3 1.0
CA A:ASP351 4.7 39.0 1.0
C A:THR625 4.8 56.0 1.0
C A:THR353 4.8 63.0 1.0
C A:ASP351 4.8 56.4 1.0
C A:THR181 4.9 51.4 1.0
O A:ILE624 4.9 45.4 1.0
CB A:LYS352 4.9 49.0 1.0
CA A:GLY626 5.0 38.1 1.0

Reference:

J.D.Clausen, M.Bublitz, B.Arnou, C.Olesen, J.P.Andersen, J.D.Clausen, M.Bublitz, B.Arnou, C.Olesen, J.P.Andersen, J.V.Moller, P.Nissen. Crystal Structure of the Vanadate-Inhibited Ca(2+)-Atpase. Structure V. 24 617 2016.
ISSN: ISSN 0969-2126
PubMed: 27050689
DOI: 10.1016/J.STR.2016.02.018
Page generated: Fri Oct 11 19:54:56 2024

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