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2FYP

GRP94 in complex with the novel HSP90 Inhibitor Radester amine

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
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE RDE A 1001
ChainResidue
AASN107
AALA111
AASP149
AMET154
APHE199
ATHR245
AILE247
AHOH1005
AHOH1006

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE RDE B 1002
ChainResidue
BASN107
BALA111
BASP149
BGLY153
BMET154
BPHE199
BTHR245
BILE247
BHOH1007
BHOH1009

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 A 501
ChainResidue
ATHR212
AARG237
ATHR248
AHOH1178

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 A 502
ChainResidue
ALYS137
ATHR148
ATRP282
AHOH1097
AHOH1170

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 A 503
ChainResidue
AASP110
ALYS114
ALEU117
AHOH1168

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 B 504
ChainResidue
BTHR212
BARG237
BTHR240
BTHR248
BHOH1024

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PG4 B 505
ChainResidue
BLYS137
BHIS146
BTHR148
BTRP282
BHOH1003
BHOH1125
BHOH1151

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PG4 B 506
ChainResidue
BASP262
BASN266

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PG4 B 507
ChainResidue
BASP110
BLYS114
BLEU117

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 A 508
ChainResidue
AGLY128
AASN129
AASN239
AHOH1048

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 1PE B 601
ChainResidue
AASN83
ALYS87
ASER227
AHOH1060
BASN83
BLYS87
BILE90
BSER227
BHOH1157
BHOH1168

Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YkNKEIFLRE
ChainResidueDetails
ATYR94-GLU103

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:1YT0, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V
ChainResidueDetails
AASN107
BASN107

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TBW, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:1YT0, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V
ChainResidueDetails
AASP149
APHE199
BASP149
BPHE199

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TBW, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V
ChainResidueDetails
AASN162
BASN162

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P14625
ChainResidueDetails
ALYS168
BLYS168

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q66HD0
ChainResidueDetails
ASER172
BSER172

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by CK2 => ECO:0000255
ChainResidueDetails
AGLY325
BGLY325

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P14625, ECO:0000255
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN107
AASN217
BASN107
BASN217

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PDB entries from 2025-06-18

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