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Chlorine in PDB 1ome: Crystal Structure of the Omega Loop Deletion Mutant (Residues 163-178 Deleted) of Beta-Lactamase From Staphylococcus Aureus PC1

Enzymatic activity of Crystal Structure of the Omega Loop Deletion Mutant (Residues 163-178 Deleted) of Beta-Lactamase From Staphylococcus Aureus PC1

All present enzymatic activity of Crystal Structure of the Omega Loop Deletion Mutant (Residues 163-178 Deleted) of Beta-Lactamase From Staphylococcus Aureus PC1:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Omega Loop Deletion Mutant (Residues 163-178 Deleted) of Beta-Lactamase From Staphylococcus Aureus PC1, PDB code: 1ome was solved by S.Banerjee, U.Pieper, O.Herzberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 76.000, 55.000, 79.200, 90.00, 90.25, 90.00
R / Rfree (%) 19 / 29.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Omega Loop Deletion Mutant (Residues 163-178 Deleted) of Beta-Lactamase From Staphylococcus Aureus PC1 (pdb code 1ome). 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 the Omega Loop Deletion Mutant (Residues 163-178 Deleted) of Beta-Lactamase From Staphylococcus Aureus PC1, PDB code: 1ome:

Chlorine binding site 1 out of 1 in 1ome

Go back to Chlorine Binding Sites List in 1ome
Chlorine binding site 1 out of 1 in the Crystal Structure of the Omega Loop Deletion Mutant (Residues 163-178 Deleted) of Beta-Lactamase From Staphylococcus Aureus PC1


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 the Omega Loop Deletion Mutant (Residues 163-178 Deleted) of Beta-Lactamase From Staphylococcus Aureus PC1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1

b:9.4
occ:1.00
 ND2 B:ASN245 3.4 18.4 1.0
N B:ARG244 3.5 28.8 1.0
N B:ASN245 3.5 27.2 1.0
CB B:ALA238 3.5 17.1 1.0
CA B:GLY236 3.5 11.9 1.0
C B:GLY236 3.7 16.8 1.0
N B:ALA238 3.7 21.5 1.0
CB B:ARG244 3.8 27.4 1.0
CA B:ARG244 4.0 30.2 1.0
N B:GLN237 4.0 18.6 1.0
CB B:ALA69 4.1 11.6 1.0
O B:GLY236 4.1 18.8 1.0
C B:ARG244 4.1 27.8 1.0
CA B:ALA238 4.2 17.4 1.0
CB B:ASN245 4.3 21.4 1.0
CG B:ASN245 4.3 18.5 1.0
CE2 B:TYR241 4.3 12.7 1.0
CA B:ASN245 4.4 22.7 1.0
N B:GLY236 4.4 12.7 1.0
C B:SER243 4.5 32.0 1.0
CA B:SER243 4.5 31.4 1.0
O B:ASN245 4.5 19.6 1.0
C B:GLN237 4.7 24.1 1.0
OH B:TYR241 4.7 15.5 1.0
CA B:GLN237 4.8 23.5 1.0
CZ B:TYR241 4.8 9.2 1.0
O B:ALA242 4.8 17.4 1.0
C B:ASN245 4.9 18.7 1.0

Reference:

S.Banerjee, U.Pieper, G.Kapadia, L.K.Pannell, O.Herzberg. Role of the Omega-Loop in the Activity, Substrate Specificity, and Structure of Class A Beta-Lactamase. Biochemistry V. 37 3286 1998.
ISSN: ISSN 0006-2960
PubMed: 9521648
DOI: 10.1021/BI972127F
Page generated: Sat Jul 20 00:58:01 2024

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