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6NSV

Crystal structure of the human CHIP TPR domain in complex with a 5mer acetylated optimized 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 Residues1
Detailsbinding site for residue CL A 201
ChainResidue
A1PE203

site_idAC2
Number of Residues5
Detailsbinding site for residue NA A 202
ChainResidue
AGLN74
AHIS76
AGLU106
AHOH302
BGLU106

site_idAC3
Number of Residues7
Detailsbinding site for residue 1PE A 203
ChainResidue
BLYS72
B1PE202
CTRP638
DTRP638
ATYR42
ALYS72
ACL201

site_idAC4
Number of Residues5
Detailsbinding site for residue NA B 201
ChainResidue
AGLU106
BGLN74
BHIS76
BGLU106
BHOH305

site_idAC5
Number of Residues4
Detailsbinding site for residue 1PE B 202
ChainResidue
A1PE203
BLYS72
CTRP638
DTRP638

site_idAC6
Number of Residues8
Detailsbinding site for Di-peptide ACE C 636 and LEU C 637
ChainResidue
ALYS95
APHE98
APHE99
APHE131
AILE135
AHOH320
CTRP638
CTRP639

site_idAC7
Number of Residues8
Detailsbinding site for Di-peptide ACE D 636 and LEU D 637
ChainResidue
AARG35
BLYS95
BPHE98
BPHE99
BPHE131
BHOH311
DTRP638
DTRP639

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER23
BSER23

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER25
ASER149
BSER25
BSER149

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PDB entries from 2024-07-17

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