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Atomistry » Chlorine » PDB 3ue5-3unf » 3ukh » |
Chlorine in PDB 3ukh: Crystal Structure of Udp-Galactopyranose Mutase From Aspergillus Fumigatus in Complex with Udpgalp (Non-Reduced)Enzymatic activity of Crystal Structure of Udp-Galactopyranose Mutase From Aspergillus Fumigatus in Complex with Udpgalp (Non-Reduced)
All present enzymatic activity of Crystal Structure of Udp-Galactopyranose Mutase From Aspergillus Fumigatus in Complex with Udpgalp (Non-Reduced):
5.4.99.9; Protein crystallography data
The structure of Crystal Structure of Udp-Galactopyranose Mutase From Aspergillus Fumigatus in Complex with Udpgalp (Non-Reduced), PDB code: 3ukh
was solved by
K.E.Van Straaten,
D.A.R.Sanders,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Udp-Galactopyranose Mutase From Aspergillus Fumigatus in Complex with Udpgalp (Non-Reduced)
(pdb code 3ukh). 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 Udp-Galactopyranose Mutase From Aspergillus Fumigatus in Complex with Udpgalp (Non-Reduced), PDB code: 3ukh: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 3ukhGo back to Chlorine Binding Sites List in 3ukh
Chlorine binding site 1 out
of 2 in the Crystal Structure of Udp-Galactopyranose Mutase From Aspergillus Fumigatus in Complex with Udpgalp (Non-Reduced)
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 3ukhGo back to Chlorine Binding Sites List in 3ukh
Chlorine binding site 2 out
of 2 in the Crystal Structure of Udp-Galactopyranose Mutase From Aspergillus Fumigatus in Complex with Udpgalp (Non-Reduced)
Mono view Stereo pair view
Reference:
K.E.Van Straaten,
F.H.Routier,
D.A.Sanders.
Structural Insight Into the Unique Substrate Binding Mechanism and Flavin Redox State of Udp-Galactopyranose Mutase From Aspergillus Fumigatus. J.Biol.Chem. V. 287 10780 2012.
Page generated: Sat Dec 12 10:15:12 2020
ISSN: ISSN 0021-9258 PubMed: 22334662 DOI: 10.1074/JBC.M111.322974 |
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