Chlorine in PDB 3pl0: Crystal Structure of A Bsma Homolog (MPE_A2762) From Methylobium Petroleophilum PM1 at 1.91 A Resolution

The structure of Crystal Structure of A Bsma Homolog (MPE_A2762) From Methylobium Petroleophilum PM1 at 1.91 A Resolution, PDB code: 3pl0 was solved by Joint Center For Structural Genomics (Jcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.92 / 1.91
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	43.508, 63.203, 104.504, 90.00, 97.80, 90.00
R / Rfree (%)	16.9 / 21.1

The binding sites of Chlorine atom in the Crystal Structure of A Bsma Homolog (MPE_A2762) From Methylobium Petroleophilum PM1 at 1.91 A Resolution (pdb code 3pl0). 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 A Bsma Homolog (MPE_A2762) From Methylobium Petroleophilum PM1 at 1.91 A Resolution, PDB code: 3pl0:

Chlorine binding site 1 out of 1 in the Crystal Structure of A Bsma Homolog (MPE_A2762) From Methylobium Petroleophilum PM1 at 1.91 A Resolution


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 A Bsma Homolog (MPE_A2762) From Methylobium Petroleophilum PM1 at 1.91 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl255 b:63.1 occ:1.00 NH1 A:ARG166 3.5 40.7 1.0 NH2 A:ARG166 3.7 35.7 1.0 O A:GLY168 3.9 33.0 1.0 CZ A:ARG166 4.1 40.5 1.0 NE2 A:GLN250 4.1 57.9 1.0 C A:GLY168 4.2 37.0 1.0 CA A:GLY168 4.4 38.0 1.0 CB A:TYR95 4.5 41.0 1.0 O A:TYR95 4.8 38.3 1.0 NH2 A:ARG245 4.8 46.9 1.0

Q.Xu, J.Grant, H.J.Chiu, C.L.Farr, L.Jaroszewski, M.W.Knuth, M.D.Miller, S.A.Lesley, A.Godzik, M.A.Elsliger, A.M.Deacon, I.A.Wilson. Crystal Structure of A Member of A Novel Family of Dioxygenases (PF10014) Reveals A Conserved Cupin Fold and Active Site. Proteins V. 82 164 2014.
ISSN: ISSN 0887-3585
PubMed: 23852666
DOI: 10.1002/PROT.24362