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Atomistry » Chlorine » PDB 6m7z-6miy » 6m8w | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 6m7z-6miy » 6m8w » |
Chlorine in PDB 6m8w: Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor AiafEnzymatic activity of Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Aiaf
All present enzymatic activity of Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Aiaf:
3.4.21.100; Protein crystallography data
The structure of Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Aiaf, PDB code: 6m8w
was solved by
A.Wlodawer,
M.Li,
A.Gustchina,
Z.Dauter,
K.Uchida,
H.Oyama,
N.E.Goldfarb,
B.M.Dunn,
K.Oda,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6m8w:
The structure of Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Aiaf also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Aiaf
(pdb code 6m8w). 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 Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Aiaf, PDB code: 6m8w: Chlorine binding site 1 out of 1 in 6m8wGo back to Chlorine Binding Sites List in 6m8w
Chlorine binding site 1 out
of 1 in the Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Aiaf
Mono view Stereo pair view
Reference:
A.Wlodawer,
M.Li,
A.Gustchina,
Z.Dauter,
K.Uchida,
H.Oyama,
N.E.Goldfarb,
B.M.Dunn,
K.Oda.
Inhibitor Complexes of the Pseudomonas Serine-Carboxyl Proteinase Biochemistry V. 40 15602 2001.
Page generated: Sun Jul 28 03:07:23 2024
ISSN: ISSN 0006-2960 PubMed: 11747435 DOI: 10.1021/BI011817N |
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