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Atomistry » Calcium » PDB 1h80-1hny » 1hax » |
Calcium in PDB 1hax: Snapshots of Serine Protease Catalysis: (A) Acyl-Enzyme Intermediate Between Porcine Pancreatic Elastase and Human Beta-Casomorphin-7 at pH 5Enzymatic activity of Snapshots of Serine Protease Catalysis: (A) Acyl-Enzyme Intermediate Between Porcine Pancreatic Elastase and Human Beta-Casomorphin-7 at pH 5
All present enzymatic activity of Snapshots of Serine Protease Catalysis: (A) Acyl-Enzyme Intermediate Between Porcine Pancreatic Elastase and Human Beta-Casomorphin-7 at pH 5:
3.4.21.11; Protein crystallography data
The structure of Snapshots of Serine Protease Catalysis: (A) Acyl-Enzyme Intermediate Between Porcine Pancreatic Elastase and Human Beta-Casomorphin-7 at pH 5, PDB code: 1hax
was solved by
R.C.Wilmouth,
K.Edman,
R.Neutze,
P.A.Wright,
I.J.Clifton,
T.R.Schneider,
C.J.Schofield,
J.Hajdu,
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 Snapshots of Serine Protease Catalysis: (A) Acyl-Enzyme Intermediate Between Porcine Pancreatic Elastase and Human Beta-Casomorphin-7 at pH 5
(pdb code 1hax). 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 Snapshots of Serine Protease Catalysis: (A) Acyl-Enzyme Intermediate Between Porcine Pancreatic Elastase and Human Beta-Casomorphin-7 at pH 5, PDB code: 1hax: Calcium binding site 1 out of 1 in 1haxGo back to Calcium Binding Sites List in 1hax
Calcium binding site 1 out
of 1 in the Snapshots of Serine Protease Catalysis: (A) Acyl-Enzyme Intermediate Between Porcine Pancreatic Elastase and Human Beta-Casomorphin-7 at pH 5
Mono view Stereo pair view
Reference:
R.C.Wilmouth,
K.Edman,
R.Neutze,
P.A.Wright,
I.J.Clifton,
T.R.Schneider,
C.J.Schofield,
J.Hajdu.
X-Ray Snapshots of Serine Protease Catalysis Reveal A Tetrahedral Intermediate Nat.Struct.Biol. V. 8 689 2001.
Page generated: Thu Jul 11 10:00:00 2024
ISSN: ISSN 1072-8368 PubMed: 11473259 DOI: 10.1038/90401 |
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