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2VW5

Structure Of The Hsp90 Inhibitor 7-O-carbamoylpremacbecin Bound To The N- Terminus Of Yeast Hsp90

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
B0005524molecular_functionATP binding
B0006457biological_processprotein folding
B0016887molecular_functionATP hydrolysis activity
B0051082molecular_functionunfolded protein binding
B0140662molecular_functionATP-dependent protein folding chaperone
C0005524molecular_functionATP binding
C0006457biological_processprotein folding
C0016887molecular_functionATP hydrolysis activity
C0051082molecular_functionunfolded protein binding
C0140662molecular_functionATP-dependent protein folding chaperone
D0005524molecular_functionATP binding
D0006457biological_processprotein folding
D0016887molecular_functionATP hydrolysis activity
D0051082molecular_functionunfolded protein binding
D0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE BC6 A 500
ChainResidue
AASN37
AGLY121
AVAL122
AGLY123
APHE124
ATHR171
AHOH2055
AHOH2113
AHOH2114
AASP40
AALA41
ALYS44
AASP79
AILE82
AASN92
ALEU93
ALYS98

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE BC6 B 500
ChainResidue
BASN37
BASP40
BALA41
BASP79
BILE82
BGLU88
BASN92
BLEU93
BGLY121
BVAL122
BGLY123
BPHE124
BTHR171
BHOH2028
BHOH2062
BHOH2124
BHOH2125
BHOH2126

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE BC6 C 500
ChainResidue
CASN37
CASP40
CALA41
CLYS44
CASP79
CILE82
CASN92
CLEU93
CGLY121
CVAL122
CGLY123
CPHE124
CTHR171
CHOH2018
CHOH2050
CHOH2107
CHOH2108

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE BC6 D 500
ChainResidue
DASN37
DASP40
DALA41
DLYS44
DASP79
DILE82
DASN92
DLEU93
DGLY121
DVAL122
DGLY123
DPHE124
DTHR171
DHOH2035
DHOH2096
DHOH2097

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A1215
ChainResidue
AARG65
AARG78
AGLU165
AHOH2115
DLYS69
DGLN72

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C1215
ChainResidue
BLYS69
BGLN72
CARG78
CGLU165

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D1215
ChainResidue
ALYS69
AGLN72
AHOH2048
DARG65
DARG78
DGLU165

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C1216
ChainResidue
CLYS98
CSER99

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B1215
ChainResidue
BARG65
BARG78
BGLU165
CLYS69

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A1216
ChainResidue
ALYS98
ASER99
DLYS102

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D1216
ChainResidue
ALYS102
DLYS98
DSER99

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B1216
ChainResidue
CLYS102
BLYS98
BSER99
BHOH2069

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A1217
ChainResidue
AGLU149
AASN151
ASER155
APHE156
ATHR157
AHOH2084

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 Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:16625188, ECO:0007744|PDB:2CG9
ChainResidueDetails
AGLU33
BLYS98
BSER99
BTHR171
CGLU33
CMET84
CASN92
CLYS98
CSER99
CTHR171
DGLU33
AMET84
DMET84
DASN92
DLYS98
DSER99
DTHR171
AASN92
ALYS98
ASER99
ATHR171
BGLU33
BMET84
BASN92

site_idSWS_FT_FI2
Number of Residues12
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
DASN37
DASP79
DGLN119
AASP79
AGLN119
BASN37
BASP79
BGLN119
CASN37
CASP79
CGLN119

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PDB entries from 2024-03-27

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