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PDBsum entry 1vbt

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protein ligands Protein-protein interface(s) links
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
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
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
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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