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Atomistry » Calcium » PDB 1mts-1n7d » 1n29 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 1mts-1n7d » 1n29 » |
Calcium in PDB 1n29: Crystal Structure of the N1A Mutant of Human Group Iia Phospholipase A2Enzymatic activity of Crystal Structure of the N1A Mutant of Human Group Iia Phospholipase A2
All present enzymatic activity of Crystal Structure of the N1A Mutant of Human Group Iia Phospholipase A2:
3.1.1.4; Protein crystallography data
The structure of Crystal Structure of the N1A Mutant of Human Group Iia Phospholipase A2, PDB code: 1n29
was solved by
S.H.Edwards,
D.Thompson,
S.F.Baker,
S.P.Wood,
D.C.Wilton,
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 of the N1A Mutant of Human Group Iia Phospholipase A2
(pdb code 1n29). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of the N1A Mutant of Human Group Iia Phospholipase A2, PDB code: 1n29: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 1n29Go back to![]() ![]()
Calcium binding site 1 out
of 2 in the Crystal Structure of the N1A Mutant of Human Group Iia Phospholipase A2
![]() Mono view ![]() Stereo pair view
Calcium binding site 2 out of 2 in 1n29Go back to![]() ![]()
Calcium binding site 2 out
of 2 in the Crystal Structure of the N1A Mutant of Human Group Iia Phospholipase A2
![]() Mono view ![]() Stereo pair view
Reference:
S.H.Edwards,
D.Thompson,
S.F.Baker,
S.P.Wood,
D.C.Wilton.
The Crystal Structure of the H48Q Active Site Mutant of Human Group Iia Secreted Phospholipase A2 at 1.5 A Resolution Provides An Insight Into the Catalytic Mechanism Biochemistry V. 41 15468 2002.
Page generated: Thu Jul 11 12:39:44 2024
ISSN: ISSN 0006-2960 PubMed: 12501175 DOI: 10.1021/BI020485Z |
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