Chlorine in PDB 1yfk: Crystal Structure of Human B Type Phosphoglycerate Mutase

All present enzymatic activity of Crystal Structure of Human B Type Phosphoglycerate Mutase:
3.1.3.13; 5.4.2.1; 5.4.2.4;

The structure of Crystal Structure of Human B Type Phosphoglycerate Mutase, PDB code: 1yfk was solved by Y.Wang, Z.Wei, L.Liu, W.Gong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.07 / 2.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.861, 65.745, 124.812, 90.00, 94.36, 90.00
R / Rfree (%)	21.6 / 25.5

The binding sites of Chlorine atom in the Crystal Structure of Human B Type Phosphoglycerate Mutase (pdb code 1yfk). 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 B Type Phosphoglycerate Mutase, PDB code: 1yfk:

Chlorine binding site 1 out of 1 in the Crystal Structure of Human B Type Phosphoglycerate Mutase


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 B Type Phosphoglycerate Mutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl263 b:22.7 occ:1.00 NH2 B:ARG83 3.0 13.3 1.0 NH2 A:ARG83 3.1 15.4 1.0 NH1 B:ARG83 3.3 16.1 1.0 NH1 A:ARG83 3.3 17.7 1.0 NE1 B:TRP68 3.5 19.9 1.0 CZ B:ARG83 3.6 15.3 1.0 NE1 A:TRP68 3.6 17.3 1.0 CZ A:ARG83 3.7 17.7 1.0 CG2 A:VAL81 3.8 7.0 1.0 CB A:VAL81 3.9 9.4 1.0 CG2 B:VAL81 3.9 10.7 1.0 CB B:VAL81 4.0 11.3 1.0 CG1 A:VAL81 4.2 5.1 1.0 CG1 B:VAL81 4.2 8.5 1.0 CE2 B:TRP68 4.4 18.8 1.0 CD1 B:TRP68 4.4 20.1 1.0 CE2 A:TRP68 4.4 17.6 1.0 CD1 A:TRP68 4.5 18.2 1.0 CZ2 B:TRP68 4.6 20.1 1.0 CZ2 A:TRP68 4.7 17.7 1.0 NE B:ARG83 4.9 15.4 1.0 NE A:ARG83 5.0 17.3 1.0

Y.Wang, Z.Wei, L.Liu, Z.Cheng, Y.Lin, F.Ji, W.Gong. Crystal Structure of Human B-Type Phosphoglycerate Mutase Bound with Citrate. Biochem.Biophys.Res.Commun. V. 331 1207 2005.
ISSN: ISSN 0006-291X
PubMed: 15883004
DOI: 10.1016/J.BBRC.2005.03.243