|
Atomistry » Calcium » PDB 1ai7-1au9 » 1amh | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 1ai7-1au9 » 1amh » |
Calcium in PDB 1amh: Uncomplexed Rat Trypsin Mutant with Asp 189 Replaced with Ser (D189S)Enzymatic activity of Uncomplexed Rat Trypsin Mutant with Asp 189 Replaced with Ser (D189S)
All present enzymatic activity of Uncomplexed Rat Trypsin Mutant with Asp 189 Replaced with Ser (D189S):
3.4.21.4; Protein crystallography data
The structure of Uncomplexed Rat Trypsin Mutant with Asp 189 Replaced with Ser (D189S), PDB code: 1amh
was solved by
E.Szabo,
Z.S.Bocskei,
G.Naray-Szabo,
L.Graf,
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 Uncomplexed Rat Trypsin Mutant with Asp 189 Replaced with Ser (D189S)
(pdb code 1amh). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Uncomplexed Rat Trypsin Mutant with Asp 189 Replaced with Ser (D189S), PDB code: 1amh: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 1amhGo back to Calcium Binding Sites List in 1amh
Calcium binding site 1 out
of 2 in the Uncomplexed Rat Trypsin Mutant with Asp 189 Replaced with Ser (D189S)
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 1amhGo back to Calcium Binding Sites List in 1amh
Calcium binding site 2 out
of 2 in the Uncomplexed Rat Trypsin Mutant with Asp 189 Replaced with Ser (D189S)
Mono view Stereo pair view
Reference:
E.Szabo,
Z.Bocskei,
G.Naray-Szabo,
L.Graf.
The Three-Dimensional Structure of ASP189SER Trypsin Provides Evidence For An Inherent Structural Plasticity of the Protease. Eur.J.Biochem. V. 263 20 1999.
Page generated: Thu Jul 11 05:58:10 2024
ISSN: ISSN 0014-2956 PubMed: 10429182 DOI: 10.1046/J.1432-1327.1999.00452.X |
Last articlesMg in 4Y52Mg in 4Y30 Mg in 4Y2V Mg in 4Y2X Mg in 4Y2Y Mg in 4Y2U Mg in 4Y2T Mg in 4Y2Q Mg in 4Y2R Mg in 4Y2S |
© Copyright 2008-2020 by atomistry.com | ||
Home | Site Map | Copyright | Contact us | Privacy |