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PDBsum entry 1vbt
Go to PDB code:
Isomerase/isomerase substrate
PDB id
1vbt
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Contents
Protein chains
164 a.a.
*
Ligands
ALA-ALT-PRO-PHE-
NIT
×2
Waters
×204
*
Residue conservation analysis
PDB id:
1vbt
Links
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CSA
ProSAT
Name:
Isomerase/isomerase substrate
Title:
Structure of cyclophilin complexed with sulfur-substituted tetrapeptide aapf
Structure:
Cyclophilin a. Chain: a, b. Engineered: yes. Sulfur-substituted tetrapeptide. Chain: c, d. Engineered: yes
Source:
Homo sapiens. Human. Organism_taxid: 9606. Cell_line: xa-90 f'. Gene: cyclophilin. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: xa-90 f'. Synthetic: yes.
Biol. unit:
Tetramer (from
PQS
)
Resolution:
2.30Å
R-factor:
0.198
R-free:
0.246
Authors:
Y.Zhao,Y.Chen,M.Schutkowski,G.Fischer,H.Ke
Key ref:
Y.Zhao et al. Insight into conversion of substrate to inhibitor.
To be published
, .
Date:
16-Jun-98
Release date:
13-Jan-99
PROCHECK
Headers
References
Protein chains
?
P62937
(PPIA_HUMAN) - Peptidyl-prolyl cis-trans isomerase A from Homo sapiens
Seq:
Struc:
165 a.a.
164 a.a.
Key:
PfamA domain
Secondary structure
CATH domain
Enzyme reactions
Enzyme class:
E.C.5.2.1.8
- peptidylprolyl isomerase.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Reaction:
[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Peptidylproline (omega=180)
=
peptidylproline (omega=0)
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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