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Atomistry » Chlorine » PDB 3mmd-3mvt » 3mr1 » |
Chlorine in PDB 3mr1: Crystal Structure of Methionine Aminopeptidase From Rickettsia ProwazekiiEnzymatic activity of Crystal Structure of Methionine Aminopeptidase From Rickettsia Prowazekii
All present enzymatic activity of Crystal Structure of Methionine Aminopeptidase From Rickettsia Prowazekii:
3.4.11.18; Protein crystallography data
The structure of Crystal Structure of Methionine Aminopeptidase From Rickettsia Prowazekii, PDB code: 3mr1
was solved by
Seattle Structural Genomics Center For Infectious Disease (Ssgcid),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3mr1:
The structure of Crystal Structure of Methionine Aminopeptidase From Rickettsia Prowazekii also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Methionine Aminopeptidase From Rickettsia Prowazekii
(pdb code 3mr1). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Methionine Aminopeptidase From Rickettsia Prowazekii, PDB code: 3mr1: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 3mr1Go back to![]() ![]()
Chlorine binding site 1 out
of 2 in the Crystal Structure of Methionine Aminopeptidase From Rickettsia Prowazekii
![]() Mono view ![]() Stereo pair view
Chlorine binding site 2 out of 2 in 3mr1Go back to![]() ![]()
Chlorine binding site 2 out
of 2 in the Crystal Structure of Methionine Aminopeptidase From Rickettsia Prowazekii
![]() Mono view ![]() Stereo pair view
Reference:
T.R.Helgren,
C.Chen,
P.Wangtrakuldee,
T.E.Edwards,
B.L.Staker,
J.Abendroth,
B.Sankaran,
N.A.Housley,
P.J.Myler,
J.P.Audia,
J.R.Horn,
T.J.Hagen.
Rickettsia Prowazekii Methionine Aminopeptidase As A Promising Target For the Development of Antibacterial Agents. Bioorg.Med.Chem. V. 25 813 2017.
Page generated: Fri Jul 11 07:57:08 2025
ISSN: ISSN 0968-0896 PubMed: 28089350 DOI: 10.1016/J.BMC.2016.11.013 |
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