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PDBsum entry 3ntp

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protein ligands links
Isomerase/isomerase inhibitor PDB id
3ntp
Jmol
Contents
Protein chain
147 a.a.
Ligands
RZD
PE8
Waters ×86
PDB id:
3ntp
Name: Isomerase/isomerase inhibitor
Title: Human pin1 complexed with reduced amide inhibitor
Structure: Peptidyl-prolyl cis-trans isomerase nima-interact chain: a. Synonym: peptidyl-prolyl cis-trans isomerase pin1, ppiase p rotamase pin1. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pin1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.76Å     R-factor:   0.233     R-free:   0.266
Authors: Y.Zhang
Key ref: G.G.Xu et al. (2011). A reduced-amide inhibitor of Pin1 binds in a conformation resembling a twisted-amide transition state. Biochemistry, 50, 9545-9550. PubMed id: 21980916 DOI: 10.1021/bi201055c
Date:
05-Jul-10     Release date:   04-Jan-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q13526  (PIN1_HUMAN) -  Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
Seq:
Struc:
163 a.a.
147 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     metabolic process   15 terms 
  Biochemical function     protein binding     7 terms  

 

 
    Added reference    
 
 
DOI no: 10.1021/bi201055c Biochemistry 50:9545-9550 (2011)
PubMed id: 21980916  
 
 
A reduced-amide inhibitor of Pin1 binds in a conformation resembling a twisted-amide transition state.
G.G.Xu, Y.Zhang, A.Y.Mercedes-Camacho, F.A.Etzkorn.
 
  ABSTRACT  
 
No abstract given.

 

 

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