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6EFK

Crystal structure of the human CHIP TPR domain in complex with a 5mer acetylated HSP70 peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000209biological_processprotein polyubiquitination
A0061630molecular_functionubiquitin protein ligase activity
B0000209biological_processprotein polyubiquitination
B0061630molecular_functionubiquitin protein ligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue NA A 201
ChainResidue
AGLN32
AARG35
AARG128
AHOH324
AHOH424

site_idAC2
Number of Residues10
Detailsbinding site for Di-peptide ACE C 636 and ILE C 637
ChainResidue
BPHE99
BPHE131
BASP134
CGLU638
CGLU639
CHOH706
AARG40
AARG153
BLYS95
BPHE98

site_idAC3
Number of Residues9
Detailsbinding site for Di-peptide ACE D 636 and ILE D 637
ChainResidue
ALYS95
APHE98
APHE99
APHE131
AASP134
BARG40
DGLU638
DGLU639
DHOH704

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues66
DetailsRepeat: {"description":"TPR 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues66
DetailsRepeat: {"description":"TPR 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues64
DetailsRepeat: {"description":"TPR 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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