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PDBsum entry 2fyp

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protein ligands Protein-protein interface(s) links
Chaperone PDB id
2fyp

 

 

 

 

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Contents
Protein chains
232 a.a. *
Ligands
RDE ×2
PG4 ×8
1PE
Waters ×365
* Residue conservation analysis
PDB id:
2fyp
Name: Chaperone
Title: Grp94 in complex with the novel hsp90 inhibitor radester amine
Structure: Endoplasmin. Chain: a, b. Fragment: n-terminal domain, residues (69-337). Synonym: 94 kda glucose-regulated protein, grp94. Engineered: yes. Mutation: yes
Source: Canis lupus. Dog. Organism_taxid: 9615. Strain: familiaris. Gene: tra1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
1.95Å     R-factor:   0.230     R-free:   0.265
Authors: R.M.Immormino,D.T.Gewirth
Key ref: R.M.Immormino et al. Inhibittory ligands adopt different conformations when bound to hsp90 or grp94: implications for paralog-Specific drug design. To be published, .
Date:
08-Feb-06     Release date:   06-Feb-07    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P41148  (ENPL_CANLF) -  Endoplasmin from Canis lupus familiaris
Seq:
Struc:
 
Seq:
Struc:
804 a.a.
232 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 12 residue positions (black crosses)

 

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