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PDBsum entry 5b3z

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protein ligands Protein-protein interface(s) links
Isomerase,sugar binding protein PDB id
5b3z

 

 

 

 

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Contents
Protein chains
402 a.a.
Ligands
GLC-GLC ×4
Waters ×1117
PDB id:
5b3z
Name: Isomerase,sugar binding protein
Title: Crystal structure of hpin1 ww domain (5-39) fused with maltose-binding protein
Structure: Peptidyl-prolyl cis-trans isomerase nima-interacting 1, maltose-binding periplasmic protein. Chain: a, b, c, d. Fragment: unp(q13526) 5-39,unp(p0aex9) residues 27-393. Engineered: yes. Mutation: yes
Source: Homo sapiens, escherichia coli k-12. Human. Organism_taxid: 9606, 83333. Strain: k-12. Gene: pin1, male. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.30Å     R-factor:   0.183     R-free:   0.224
Authors: Y.Hanazono,K.Takeda,K.Miki
Key ref: Y.Hanazono et al. (2016). Structural studies of the N-terminal fragments of the WW domain: Insights into co-translational folding of a beta-sheet protein. Sci Rep, 6, 34654. PubMed id: 27698466 DOI: 10.1038/srep34654
Date:
17-Mar-16     Release date:   26-Oct-16    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0AEX9  (MALE_ECOLI) -  Maltose/maltodextrin-binding periplasmic protein from Escherichia coli (strain K12)
Seq:
Struc:
396 a.a.
402 a.a.*
Protein chains
Pfam   ArchSchema ?
Q13526  (PIN1_HUMAN) -  Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 from Homo sapiens
Seq:
Struc:
163 a.a.
402 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 142 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 2: 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)
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1038/srep34654 Sci Rep 6:34654 (2016)
PubMed id: 27698466  
 
 
Structural studies of the N-terminal fragments of the WW domain: Insights into co-translational folding of a beta-sheet protein.
Y.Hanazono, K.Takeda, K.Miki.
 
  ABSTRACT  
 
No abstract given.

 

 

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