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Atomistry » Chlorine » PDB 4ote-4oz0 » 4oxd » |
Chlorine in PDB 4oxd: Structure of the Ldcb Ld-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan RecognitionProtein crystallography data
The structure of Structure of the Ldcb Ld-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan Recognition, PDB code: 4oxd
was solved by
C.N.Hoyland,
C.Aldridge,
R.M.Cleverley,
K.Sidiq,
M.C.Duchene,
R.A.Daniel,
W.Vollmer,
R.J.Lewis,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4oxd:
The structure of Structure of the Ldcb Ld-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan Recognition also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Structure of the Ldcb Ld-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan Recognition
(pdb code 4oxd). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of the Ldcb Ld-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan Recognition, PDB code: 4oxd: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 4oxdGo back to Chlorine Binding Sites List in 4oxd
Chlorine binding site 1 out
of 2 in the Structure of the Ldcb Ld-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan Recognition
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 4oxdGo back to Chlorine Binding Sites List in 4oxd
Chlorine binding site 2 out
of 2 in the Structure of the Ldcb Ld-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan Recognition
Mono view Stereo pair view
Reference:
C.N.Hoyland,
C.Aldridge,
R.M.Cleverley,
M.C.Duchene,
G.Minasov,
O.Onopriyenko,
K.Sidiq,
P.J.Stogios,
W.F.Anderson,
R.A.Daniel,
A.Savchenko,
W.Vollmer,
R.J.Lewis.
Structure of the Ldcb Ld-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan Recognition. Structure V. 22 949 2014.
Page generated: Sat Dec 12 11:02:01 2020
ISSN: ISSN 0969-2126 PubMed: 24909784 DOI: 10.1016/J.STR.2014.04.015 |
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