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6U98

Hsp90a NTD K58R bound reversibly to sulfonyl fluoride 6

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 Q2D A 301
ChainResidue
AASN51
APHE134
AGLY135
APHE138
ATYR139
ATRP162
ATHR184
AHOH407
AHOH421
AHOH425
AHOH450
AALA55
AHOH463
AHOH472
AHOH520
AHOH534
AASP57
AARG60
ATYR61
AASP93
AMET98
ALEU107
AILE110

site_idAC2
Number of Residues4
Detailsbinding site for residue K A 302
ChainResidue
AILE81
ATHR88
ATHR90
AHOH651

site_idAC3
Number of Residues4
Detailsbinding site for residue NA A 303
ChainResidue
ASER50
AASP54
AHOH558
AHOH660

Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR38-GLU47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AASN51
AASP93
APHE138

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS112

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PRKDC => ECO:0000269|PubMed:2507541
ChainResidueDetails
ATHR5
ATHR7

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07901
ChainResidueDetails
AARG58
ALYS84

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:2492519, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER231

222415

PDB entries from 2024-07-10

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