Chlorine in PDB 4gpi: 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: 4gpi was solved by L.Zhou, C.He, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.62 / 2.08
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	81.662, 80.263, 89.275, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 23.3

The binding sites of Chlorine atom in the Crystal Structure of Human B Type Phosphoglycerate Mutase (pdb code 4gpi). 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: 4gpi:

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 B:Cl301 b:21.3 occ:1.00 NH1 B:ARG83 3.2 16.3 1.0 NH2 C:ARG83 3.2 19.0 1.0 NH1 C:ARG83 3.2 19.8 1.0 NH2 B:ARG83 3.3 18.2 1.0 NE1 C:TRP68 3.4 19.1 1.0 NE1 B:TRP68 3.4 20.7 1.0 CZ C:ARG83 3.7 22.6 1.0 CZ B:ARG83 3.7 22.7 1.0 CG2 C:VAL81 4.0 19.0 1.0 CB C:VAL81 4.0 19.8 1.0 CB B:VAL81 4.1 19.5 1.0 CG2 B:VAL81 4.1 20.8 1.0 CE2 C:TRP68 4.2 18.5 1.0 CD1 B:TRP68 4.3 20.1 1.0 CG1 C:VAL81 4.3 22.9 1.0 CG1 B:VAL81 4.3 16.6 1.0 CE2 B:TRP68 4.3 21.3 1.0 CD1 C:TRP68 4.3 21.7 1.0 CZ2 C:TRP68 4.4 22.1 1.0 CZ2 B:TRP68 4.6 23.3 1.0

T.Hitosugi, L.Zhou, J.Fan, S.Elf, L.Zhang, J.Xie, Y.Wang, T.L.Gu, M.Aleckovic, G.Leroy, Y.Kang, H.B.Kang, J.H.Seo, C.Shan, P.Jin, W.Gong, S.Lonial, M.L.Arellano, H.J.Khoury, G.Z.Chen, D.M.Shin, F.R.Khuri, T.J.Boggon, S.Kang, C.He, J.Chen. TYR26 Phosphorylation of PGAM1 Provides A Metabolic Advantage to Tumours By Stabilizing the Active Conformation. Nat Commun V. 4 1790 2013.
ISSN: ESSN 2041-1723
PubMed: 23653202
DOI: 10.1038/NCOMMS2759