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6GQS

Structure of human Heat shock protein 90-alpha N-terminal domain (Hsp90-NTD) variant K112R in complex with AMPCP

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 Residues26
Detailsbinding site for residue A12 A 301
ChainResidue
AASN51
AGLY137
APHE138
ATHR184
AMG303
AHOH406
AHOH424
AHOH450
AHOH452
AHOH456
AHOH461
AALA55
AHOH467
AHOH480
AHOH481
AHOH527
AHOH536
AHOH572
AHOH634
AASP93
AMET98
AASN106
ALEU107
AARG112
AGLY135
AVAL136

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 302
ChainResidue
AHOH462
AHOH468
AHOH579

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 303
ChainResidue
AASN51
AA12301
AHOH452
AHOH467
AHOH480

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
APHE138
AASN51
AASP93

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG112

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

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07901
ChainResidueDetails
ALYS58
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

220472

PDB entries from 2024-05-29

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