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PDBsum entry 3upv

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Peptide binding protein PDB id
3upv

 

 

 

 

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Contents
Protein chain
125 a.a.
Ligands
PRO-THR-VAL-GLU-
GLU-VAL-ASP
Waters ×143
PDB id:
3upv
Name: Peptide binding protein
Title: Tpr2b-domain:phsp70-complex of yeast sti1
Structure: Heat shock protein sti1. Chain: a. Fragment: tpr repeats 7-9, residues 395-518. Engineered: yes. Heat shock protein ssa4. Chain: b. Fragment: unp residues 636-642. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: sti1, yor027w, or26.17. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Saccharomyces cerevisiae s288c.
Resolution:
1.60Å     R-factor:   0.186     R-free:   0.254
Authors: A.B.Schmid,S.Lagleder,M.A.Graewert,A.Roehl,F.Hagn,S.K.Wandinger, M.B.Cox,O.Demmer,K.Richter,M.Groll,H.Kessler
Key ref: A.B.Schmid et al. (2012). The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. Embo J, 31, 1506-1517. PubMed id: 22227520
Date:
18-Nov-11     Release date:   25-Jan-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P15705  (STI1_YEAST) -  Heat shock protein STI1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
589 a.a.
125 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
Embo J 31:1506-1517 (2012)
PubMed id: 22227520  
 
 
The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop.
A.B.Schmid, S.Lagleder, M.A.Gräwert, A.Röhl, F.Hagn, S.K.Wandinger, M.B.Cox, O.Demmer, K.Richter, M.Groll, H.Kessler, J.Buchner.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23288357 G.Chiosis, C.A.Dickey, and J.L.Johnson (2013).
A global view of Hsp90 functions.
  Nat Struct Mol Biol, 20, 1-4.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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