Chlorine in PDB 4bjp: Crystal Structure of E. Coli Penicillin Binding Protein 3

Enzymatic activity of Crystal Structure of E. Coli Penicillin Binding Protein 3

All present enzymatic activity of Crystal Structure of E. Coli Penicillin Binding Protein 3:
2.4.1.129;

Protein crystallography data

The structure of Crystal Structure of E. Coli Penicillin Binding Protein 3, PDB code: 4bjp was solved by E.Sauvage, M.Joris, R.Herman, F.Kerff, M.Rocaboy, P.Charlier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 59.51 / 2.50
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 119.025, 119.025, 139.251, 90.00, 90.00, 120.00
R / Rfree (%) 19.876 / 24.493

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of E. Coli Penicillin Binding Protein 3 (pdb code 4bjp). 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 E. Coli Penicillin Binding Protein 3, PDB code: 4bjp:

Chlorine binding site 1 out of 1 in 4bjp

Go back to Chlorine Binding Sites List in 4bjp
Chlorine binding site 1 out of 1 in the Crystal Structure of E. Coli Penicillin Binding Protein 3


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 E. Coli Penicillin Binding Protein 3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl660

b:65.0
occ:1.00
OE2 A:GLU258 2.9 43.7 1.0
NZ A:LYS500 3.0 48.4 1.0
OE1 A:GLU258 3.4 43.8 1.0
CD A:GLU258 3.5 40.6 1.0
ND2 A:ASN533 3.6 35.1 1.0
CE A:LYS500 3.7 46.6 1.0
NH1 A:ARG297 4.4 33.2 1.0
NH2 A:ARG295 4.6 31.8 1.0
CG A:ASN533 4.7 32.0 1.0
OE2 A:GLU292 4.8 53.7 1.0
OD1 A:ASN533 4.9 32.9 1.0

Reference:

E.Sauvage, A.Derouaux, C.Fraipont, M.Joris, R.Herman, M.Rocaboy, M.Schloesser, J.Dumas, F.Kerff, M.Nguyen-Disteche, P.Charlier. Crystal Structure of Penicillin-Binding Protein 3 (PBP3) From Escherichia Coli. Plos One V. 9 98042 2014.
ISSN: ISSN 1932-6203
PubMed: 24875494
DOI: 10.1371/JOURNAL.PONE.0098042
Page generated: Sat Dec 12 10:26:43 2020

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