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3C11

Yeast Hsp82 N-terminal domain-Geldanamycin complex: effects of mutants 98-99 KS-AA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0006457biological_processprotein folding
A0016887molecular_functionATP hydrolysis activity
A0051082molecular_functionunfolded protein binding
A0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE GDM A 300
ChainResidue
AASN37
AGLY121
AVAL122
AGLY123
APHE124
ATHR171
AHOH402
AHOH403
AHOH406
AHOH407
AHOH439
AASP40
AHOH465
AHOH512
AHOH525
AHOH564
AALA41
ALYS44
AASP79
AILE82
AMET84
AASN92
ALEU93

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
ALYS54
AGLN55
ATHR58

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
ATHR58
AGLU59
AARG78
AGLY168
AHOH495
AHOH587
AHOH599

Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR24-GLU33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16625188, ECO:0007744|PDB:2CG9
ChainResidueDetails
AGLU33
AMET84
AASN92
AALA98
AALA99
ATHR171

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16625188, ECO:0000269|PubMed:9230303, ECO:0007744|PDB:1AM1, ECO:0007744|PDB:1AMW, ECO:0007744|PDB:2CG9, ECO:0007744|PDB:2WEP
ChainResidueDetails
AASN37
AASP79
AGLN119

223532

PDB entries from 2024-08-07

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