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Atomistry » Calcium » PDB 3f5v-3fib » 3f7o | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 3f5v-3fib » 3f7o » |
Calcium in PDB 3f7o: Crystal Structure of Cuticle-Degrading Protease From Paecilomyces Lilacinus (PL646)Protein crystallography data
The structure of Crystal Structure of Cuticle-Degrading Protease From Paecilomyces Lilacinus (PL646), PDB code: 3f7o
was solved by
L.Liang,
Z.Lou,
Z.Meng,
Z.Rao,
K.Zhang,
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 Cuticle-Degrading Protease From Paecilomyces Lilacinus (PL646)
(pdb code 3f7o). 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 Cuticle-Degrading Protease From Paecilomyces Lilacinus (PL646), PDB code: 3f7o: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 3f7oGo back to Calcium Binding Sites List in 3f7o
Calcium binding site 1 out
of 2 in the Crystal Structure of Cuticle-Degrading Protease From Paecilomyces Lilacinus (PL646)
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 3f7oGo back to Calcium Binding Sites List in 3f7o
Calcium binding site 2 out
of 2 in the Crystal Structure of Cuticle-Degrading Protease From Paecilomyces Lilacinus (PL646)
Mono view Stereo pair view
Reference:
L.Liang,
Z.Meng,
F.Ye,
J.Yang,
S.Liu,
Y.Sun,
Y.Guo,
Q.Mi,
X.Huang,
C.Zou,
Z.Rao,
Z.Lou,
K.Q.Zhang.
The Crystal Structures of Two Cuticle-Degrading Proteases From Nematophagous Fungi and Their Contribution to Infection Against Nematodes. Faseb J. V. 24 1391 2010.
Page generated: Sat Jul 13 09:43:30 2024
ISSN: ISSN 0892-6638 PubMed: 20007510 DOI: 10.1096/FJ.09-136408 |
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