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Atomistry » Calcium » PDB 6m4m-6mr8 » 6m9f | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 6m4m-6mr8 » 6m9f » |
Calcium in PDB 6m9f: Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor TyrostatinEnzymatic activity of Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Tyrostatin
All present enzymatic activity of Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Tyrostatin:
3.4.21.100; Protein crystallography data
The structure of Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Tyrostatin, PDB code: 6m9f
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:
Calcium Binding Sites:
The binding sites of Calcium atom in the Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Tyrostatin
(pdb code 6m9f). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Tyrostatin, PDB code: 6m9f: Calcium binding site 1 out of 1 in 6m9fGo back to Calcium Binding Sites List in 6m9f
Calcium binding site 1 out
of 1 in the Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Tyrostatin
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: Tue Jul 16 11:17:11 2024
ISSN: ISSN 0006-2960 PubMed: 11747435 DOI: 10.1021/BI011817N |
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