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4L93

Crystal structure of Human Hsp90 with S36

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 Residues12
DetailsBINDING SITE FOR RESIDUE S36 A 301
ChainResidue
AASN51
AVAL186
AHOH401
AHOH437
AASP54
AALA55
AASP93
AGLY97
AMET98
ALEU107
APHE138
ATHR184

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE S36 B 301
ChainResidue
BASN51
BASP54
BALA55
BASP93
BILE96
BGLY97
BPHE138
BTHR184
BVAL186
BHOH401
BHOH417

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 Residues6
DetailsBINDING:
ChainResidueDetails
AASN51
AASP93
APHE138
BASN51
BASP93
BPHE138

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS112
BLYS112

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07901
ChainResidueDetails
ALYS58
ALYS84
BLYS58
BLYS84

site_idSWS_FT_FI4
Number of Residues2
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
BSER231

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PDB entries from 2024-07-24

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