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PDBsum entry 2zqv

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protein ligands links
Isomerase PDB id
2zqv
Jmol
Contents
Protein chain
153 a.a. *
Ligands
SO4
1PG
Waters ×103
* Residue conservation analysis
PDB id:
2zqv
Name: Isomerase
Title: Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase
Structure: Peptidyl-prolyl cis-trans isomerase nima- interacting 1. Chain: a. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pin1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.222     R-free:   0.303
Authors: C.Jobichen,Y.C.Liou,J.Sivaraman
Key ref: C.Jobichen et al. Structural studies on pin1 mutants. To be published, .
Date:
20-Aug-08     Release date:   25-Aug-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q13526  (PIN1_HUMAN) -  Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
Seq:
Struc:
163 a.a.
153 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.5.2.1.8  - Peptidylprolyl isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Peptidylproline (omega=180) = peptidylproline (omega=0)
Peptidylproline (omega=180)
= peptidylproline (omega=0)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     midbody   5 terms 
  Biological process     negative regulation of cell motility   15 terms 
  Biochemical function     protein binding     7 terms