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Atomistry » Calcium » PDB 1vfo-1w7c » 1w52 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 1vfo-1w7c » 1w52 » |
Calcium in PDB 1w52: Crystal Structure of A Proteolyzed Form of Pancreatic Lipase Related Protein 2 From HorseProtein crystallography data
The structure of Crystal Structure of A Proteolyzed Form of Pancreatic Lipase Related Protein 2 From Horse, PDB code: 1w52
was solved by
J.M.Mancheno,
S.Jayne,
B.Kerfelec,
C.Chapus,
I.Crenon,
J.A.Hermoso,
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 A Proteolyzed Form of Pancreatic Lipase Related Protein 2 From Horse
(pdb code 1w52). 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 A Proteolyzed Form of Pancreatic Lipase Related Protein 2 From Horse, PDB code: 1w52: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 1w52Go back to![]() ![]()
Calcium binding site 1 out
of 2 in the Crystal Structure of A Proteolyzed Form of Pancreatic Lipase Related Protein 2 From Horse
![]() Mono view ![]() Stereo pair view
Calcium binding site 2 out of 2 in 1w52Go back to![]() ![]()
Calcium binding site 2 out
of 2 in the Crystal Structure of A Proteolyzed Form of Pancreatic Lipase Related Protein 2 From Horse
![]() Mono view ![]() Stereo pair view
Reference:
J.M.Mancheno,
S.Jayne,
B.Kerfelec,
C.Chapus,
I.Crenon,
J.A.Hermoso.
Crystalization of A Proteolyzed Form of the Horse Pancreatic Lipase-Related Protein 2: Structural Basis For the Specific Detergent Requirement. Acta Crystallogr.,Sect.D V. 60 2107 2004.
Page generated: Fri Jul 12 07:04:25 2024
ISSN: ISSN 0907-4449 PubMed: 15502342 DOI: 10.1107/S0907444904024229 |
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