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Chlorine in PDB 3v31: Crystal Structure of the Peptide Bound Complex of the Ankyrin Repeat Domains of Human ANKRA2

Enzymatic activity of Crystal Structure of the Peptide Bound Complex of the Ankyrin Repeat Domains of Human ANKRA2

All present enzymatic activity of Crystal Structure of the Peptide Bound Complex of the Ankyrin Repeat Domains of Human ANKRA2:
3.5.1.98;

Protein crystallography data

The structure of Crystal Structure of the Peptide Bound Complex of the Ankyrin Repeat Domains of Human ANKRA2, PDB code: 3v31 was solved by R.Lam, C.Xu, C.B.Bian, J.Kania, C.Bountra, J.Weigelt, C.H.Arrowsmith, A.M.Edwards, A.Bochkarev, J.Min, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.41 / 1.57
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 29.663, 52.822, 51.556, 90.00, 98.01, 90.00
R / Rfree (%) 17.4 / 20.5

Other elements in 3v31:

The structure of Crystal Structure of the Peptide Bound Complex of the Ankyrin Repeat Domains of Human ANKRA2 also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Peptide Bound Complex of the Ankyrin Repeat Domains of Human ANKRA2 (pdb code 3v31). 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 Peptide Bound Complex of the Ankyrin Repeat Domains of Human ANKRA2, PDB code: 3v31:

Chlorine binding site 1 out of 1 in 3v31

Go back to Chlorine Binding Sites List in 3v31
Chlorine binding site 1 out of 1 in the Crystal Structure of the Peptide Bound Complex of the Ankyrin Repeat Domains of Human ANKRA2


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 Peptide Bound Complex of the Ankyrin Repeat Domains of Human ANKRA2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl401

b:16.3
occ:1.00
O A:HOH535 3.2 16.7 1.0
N A:ASP229 3.3 10.3 1.0
C A:TYR227 3.3 8.6 1.0
CA A:TYR227 3.5 8.2 1.0
CB A:TYR227 3.5 8.0 1.0
CB A:ASP229 3.6 11.2 1.0
N A:ILE230 3.7 7.6 1.0
O A:TYR227 3.7 8.0 1.0
N A:THR228 3.7 9.5 1.0
CD1 A:ILE195 3.7 12.7 1.0
CG1 A:ILE195 3.8 10.4 1.0
CA A:ASP229 3.9 9.8 1.0
CG1 A:ILE230 4.1 8.1 1.0
CD1 A:TYR227 4.2 11.8 1.0
C A:THR228 4.2 10.1 1.0
CG A:TYR227 4.2 8.9 1.0
C A:ASP229 4.3 9.4 1.0
CD1 A:ILE230 4.3 7.7 1.0
CG A:ASP229 4.4 14.4 1.0
CB A:ILE230 4.4 7.0 1.0
CA A:THR228 4.5 10.8 1.0
CA A:ILE230 4.7 7.7 1.0
OD2 A:ASP229 4.8 15.9 1.0
N A:TYR227 4.9 8.0 1.0

Reference:

C.Xu, J.Jin, C.Bian, R.Lam, R.Tian, R.Weist, L.You, J.Nie, A.Bochkarev, W.Tempel, C.S.Tan, G.A.Wasney, M.Vedadi, G.D.Gish, C.H.Arrowsmith, T.Pawson, X.J.Yang, J.Min. Sequence-Specific Recognition of A Pxlpxi/L Motif By An Ankyrin Repeat Tumbler Lock. Sci.Signal. V. 5 RA39 2012.
ISSN: ESSN 1937-9145
PubMed: 22649097
DOI: 10.1126/SCISIGNAL.2002979
Page generated: Fri Jul 11 11:33:55 2025

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