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PDBsum entry 3zha

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protein ligands Protein-protein interface(s) links
Chaperone PDB id
3zha

 

 

 

 

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Contents
Protein chains
(+ 2 more) 380 a.a.
(+ 1 more) 18 a.a.
17 a.a.
16 a.a.
Ligands
SIN ×5
Waters ×222
PDB id:
3zha
Name: Chaperone
Title: Molecular basis for the action of the collagen-specific chaperone hsp47 serpinh1 and its structure-specific client recognition.
Structure: Hsp47. Chain: a, b, c, d, k, l, p, q. Fragment: residues 36-418. Synonym: serpin peptidase inhibitor, clade h (heat shock protein 47), member 1, collagen binding protein 1. Engineered: yes. Collagen model peptide 18-t8r11. Chain: e, f, g, h, i, j, m, n, o, r, s, t. Engineered: yes
Source: Canis lupus familiaris. Dog. Organism_taxid: 9615. Expressed in: escherichia coli. Expression_system_taxid: 511693. Synthetic: yes. Synthetic construct. Organism_taxid: 32630
Resolution:
2.55Å     R-factor:   0.196     R-free:   0.218
Authors: C.Widmer,J.M.Gebauer,U.Baumann
Key ref: C.Widmer et al. (2012). Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition. Proc Natl Acad Sci U S A, 109, 13243-13247. PubMed id: 22847422
Date:
20-Dec-12     Release date:   09-Jan-13    
Supersedes: 4awr
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
C7C419  (C7C419_CANLF) -  Serpin H1 from Canis lupus familiaris
Seq:
Struc:
418 a.a.
380 a.a.*
Protein chains
No UniProt id for this chain
Struc: 17 a.a.
Protein chains
No UniProt id for this chain
Struc: 16 a.a.
Protein chains
No UniProt id for this chain
Struc: 15 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
Proc Natl Acad Sci U S A 109:13243-13247 (2012)
PubMed id: 22847422  
 
 
Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition.
C.Widmer, J.M.Gebauer, E.Brunstein, S.Rosenbaum, F.Zaucke, C.Drögemüller, T.Leeb, U.Baumann.
 
  ABSTRACT  
 
No abstract given.

 

 

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