Chlorine in PDB 3nbu: Crystal Structure of Pgi Glucosephosphate Isomerase

All present enzymatic activity of Crystal Structure of Pgi Glucosephosphate Isomerase:
5.3.1.9;

The structure of Crystal Structure of Pgi Glucosephosphate Isomerase, PDB code: 3nbu was solved by T.Alber, C.Zubieta, M.Totir, A.May, N.Echols, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	89.00 / 2.05
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	69.806, 72.874, 181.851, 92.47, 97.82, 114.57
R / Rfree (%)	16.9 / 23

The binding sites of Chlorine atom in the Crystal Structure of Pgi Glucosephosphate Isomerase (pdb code 3nbu). 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 Pgi Glucosephosphate Isomerase, PDB code: 3nbu:

Chlorine binding site 1 out of 1 in the Crystal Structure of Pgi Glucosephosphate Isomerase


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 Pgi Glucosephosphate Isomerase within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl550 b:27.5 occ:1.00 OD1 D:ASP265 2.9 39.1 1.0 O D:HOH1133 3.1 36.2 1.0 N D:ALA95 3.2 17.8 1.0 CD1 D:TRP266 3.6 17.9 1.0 CA D:ARG94 3.7 19.0 1.0 CB D:ARG94 3.9 18.8 1.0 CB D:TRP266 3.9 19.4 1.0 C D:ARG94 4.0 18.3 1.0 CB D:ALA95 4.0 17.1 1.0 NZ D:LYS87 4.1 34.0 1.0 CG D:TRP266 4.2 19.7 1.0 CG D:ASP265 4.2 31.2 1.0 CA D:ALA95 4.2 17.6 1.0 N D:TRP266 4.3 20.4 1.0 CG D:ARG94 4.3 18.7 1.0 CG2 D:VAL111 4.4 32.6 1.0 CA D:TRP266 4.5 19.7 1.0 O D:ALA95 4.6 15.6 1.0 O D:ASN93 4.6 17.8 1.0 NE1 D:TRP266 4.7 20.2 1.0 C D:ASP265 4.8 22.1 1.0 OD2 D:ASP265 4.8 36.7 1.0 C D:ALA95 4.9 17.9 1.0 N D:ARG94 4.9 18.1 1.0

M.Totir, N.Echols, M.Nanao, C.L.Gee, A.Moskaleva, S.Gradia, A.T.Iavarone, J.M.Berger, A.P.May, C.Zubieta, T.Alber. Macro-to-Micro Structural Proteomics: Native Source Proteins For High-Throughput Crystallization. Plos One V. 7 32498 2012.
ISSN: ESSN 1932-6203
PubMed: 22393408
DOI: 10.1371/JOURNAL.PONE.0032498