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Chlorine in PDB 6ma1: Crystal Structure of Human O-Glcnac Transferase Bound to A Peptide From Hcf-1 Pro-Repeat 2 (11-26) and Inhibitor 4A

Enzymatic activity of Crystal Structure of Human O-Glcnac Transferase Bound to A Peptide From Hcf-1 Pro-Repeat 2 (11-26) and Inhibitor 4A

All present enzymatic activity of Crystal Structure of Human O-Glcnac Transferase Bound to A Peptide From Hcf-1 Pro-Repeat 2 (11-26) and Inhibitor 4A:
2.4.1.255;

Protein crystallography data

The structure of Crystal Structure of Human O-Glcnac Transferase Bound to A Peptide From Hcf-1 Pro-Repeat 2 (11-26) and Inhibitor 4A, PDB code: 6ma1 was solved by S.E.S.Martin, M.B.Lazarus, S.Walker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.80 / 2.75
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 100.303, 100.303, 130.301, 90.00, 90.00, 120.00
R / Rfree (%) 19.9 / 24

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human O-Glcnac Transferase Bound to A Peptide From Hcf-1 Pro-Repeat 2 (11-26) and Inhibitor 4A (pdb code 6ma1). 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 Human O-Glcnac Transferase Bound to A Peptide From Hcf-1 Pro-Repeat 2 (11-26) and Inhibitor 4A, PDB code: 6ma1:

Chlorine binding site 1 out of 1 in 6ma1

Go back to Chlorine Binding Sites List in 6ma1
Chlorine binding site 1 out of 1 in the Crystal Structure of Human O-Glcnac Transferase Bound to A Peptide From Hcf-1 Pro-Repeat 2 (11-26) and Inhibitor 4A


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 Human O-Glcnac Transferase Bound to A Peptide From Hcf-1 Pro-Repeat 2 (11-26) and Inhibitor 4A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1101

b:70.5
occ:1.00
 CL1 A:JA41101 0.0 70.5 1.0
C13 A:JA41101 1.8 66.1 1.0
C06 A:JA41101 2.8 63.5 1.0
C12 A:JA41101 2.8 64.3 1.0
H121 A:JA41101 2.9 77.2 1.0
O19 A:JA41101 3.1 74.7 1.0
S05 A:JA41101 3.3 72.5 1.0
O01 A:JA41101 3.4 70.6 1.0
N04 A:JA41101 3.5 69.6 1.0
H041 A:JA41101 3.7 83.6 1.0
CD A:LYS898 3.7 67.2 1.0
CB A:LYS898 3.9 65.8 1.0
C07 A:JA41101 4.1 61.9 1.0
CE1 A:HIS562 4.1 58.2 1.0
C02 A:JA41101 4.2 68.3 1.0
C11 A:JA41101 4.2 62.8 1.0
CA A:LYS898 4.2 64.0 1.0
CG A:LYS898 4.4 67.0 1.0
N A:LYS898 4.5 64.9 1.0
C03 A:JA41101 4.5 68.2 1.0
ND1 A:HIS562 4.6 57.2 1.0
O18 A:JA41101 4.7 74.0 1.0
C08 A:JA41101 4.7 62.6 1.0
H071 A:JA41101 4.8 74.2 1.0
H292 A:JA41101 4.8 83.0 1.0
CE A:LYS898 4.9 68.3 1.0
H031 A:JA41101 4.9 81.9 1.0
NZ A:LYS898 4.9 66.7 1.0

Reference:

S.E.S.Martin, Z.W.Tan, H.M.Itkonen, D.Y.Duveau, J.A.Paulo, J.Janetzko, P.L.Boutz, L.Tork, F.A.Moss, C.J.Thomas, S.P.Gygi, M.B.Lazarus, S.Walker. Structure-Based Evolution of Low Nanomolar O-Glcnac Transferase Inhibitors. J. Am. Chem. Soc. V. 140 13542 2018.
ISSN: ESSN 1520-5126
PubMed: 30285435
DOI: 10.1021/JACS.8B07328
Page generated: Sun Jul 28 03:07:23 2024

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