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3PRY

Crystal structure of the middle domain of human HSP90-beta refined at 2.3 A resolution

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AHOH203
ALYS411
ALYS538
AGLU539
AGLY540

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 3
ChainResidue
BGLY540
BHOH185
BLYS411
BLYS538
BGLU539

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 4
ChainResidue
BVAL318
BLYS319
BHIS320

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 5
ChainResidue
BARG506

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 6
ChainResidue
BILE370
BGLU372
BARG405

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 7
ChainResidue
BVAL403
BASN407
BLYS410
BGLU539
BLEU541
BGLU542

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 8
ChainResidue
BGLU443

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO C 9
ChainResidue
CSER434
CMET466

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"23585225","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P11499","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"source":"PubMed","id":"21908771","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P11499","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues6
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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