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Chlorine 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
Vanadium (V) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp, PDB code: 5a3q:

Chlorine binding site 1 out of 1 in 5a3q

Go back to Chlorine Binding Sites List in 5a3q
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl1009

b:65.2
occ:1.00
N A:LYS629 3.3 45.9 1.0
CD A:ARG678 3.4 42.2 1.0
CA A:ASN628 3.8 33.9 1.0
ND2 A:ASN628 3.9 54.8 1.0
CB A:ASN628 3.9 38.6 1.0
CG2 A:THR654 4.0 40.4 1.0
CB A:LYS629 4.0 41.2 1.0
C A:ASN628 4.1 50.6 1.0
CG A:ASN628 4.1 57.1 1.0
CB A:ARG678 4.1 44.9 1.0
CA A:LYS629 4.3 38.2 1.0
CG A:ARG678 4.3 49.1 1.0
NE A:ARG678 4.4 52.8 1.0
NH1 A:ARG678 4.5 85.0 1.0
CZ A:ARG678 4.8 70.0 1.0
N A:GLY630 5.0 37.6 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: Wed Oct 28 12:22:28 2020

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