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Atomistry » Calcium » PDB 1g8g-1gj6 » 1ga6 » |
Calcium in PDB 1ga6: Crystal Structure Analysis of Pscp (Pseudomonas Serine-Carboxyl Proteinase) Complexed with A Fragment of Tyrostatin (This Enzyme Renamed "Sedolisin" in 2003)Enzymatic activity of Crystal Structure Analysis of Pscp (Pseudomonas Serine-Carboxyl Proteinase) Complexed with A Fragment of Tyrostatin (This Enzyme Renamed "Sedolisin" in 2003)
All present enzymatic activity of Crystal Structure Analysis of Pscp (Pseudomonas Serine-Carboxyl Proteinase) Complexed with A Fragment of Tyrostatin (This Enzyme Renamed "Sedolisin" in 2003):
3.4.23.37; Protein crystallography data
The structure of Crystal Structure Analysis of Pscp (Pseudomonas Serine-Carboxyl Proteinase) Complexed with A Fragment of Tyrostatin (This Enzyme Renamed "Sedolisin" in 2003), PDB code: 1ga6
was solved by
A.Wlodawer,
M.Li,
Z.Dauter,
A.Gustchina,
K.Uchida,
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 Crystal Structure Analysis of Pscp (Pseudomonas Serine-Carboxyl Proteinase) Complexed with A Fragment of Tyrostatin (This Enzyme Renamed "Sedolisin" in 2003)
(pdb code 1ga6). 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 Crystal Structure Analysis of Pscp (Pseudomonas Serine-Carboxyl Proteinase) Complexed with A Fragment of Tyrostatin (This Enzyme Renamed "Sedolisin" in 2003), PDB code: 1ga6: Calcium binding site 1 out of 1 in 1ga6Go back to![]() ![]()
Calcium binding site 1 out
of 1 in the Crystal Structure Analysis of Pscp (Pseudomonas Serine-Carboxyl Proteinase) Complexed with A Fragment of Tyrostatin (This Enzyme Renamed "Sedolisin" in 2003)
![]() Mono view ![]() Stereo pair view
Reference:
A.Wlodawer,
M.Li,
Z.Dauter,
A.Gustchina,
K.Uchida,
H.Oyama,
B.M.Dunn,
K.Oda.
Carboxyl Proteinase From Pseudomonas Defines A Novel Family of Subtilisin-Like Enzymes. Nat.Struct.Biol. V. 8 442 2001.
Page generated: Thu Jul 11 08:39:04 2024
ISSN: ISSN 1072-8368 PubMed: 11323721 DOI: 10.1038/87610 |
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