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2IOR

Crystal Structure of the N-terminal Domain of HtpG, the Escherichia coli Hsp90, Bound to ADP

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 Residues5
DetailsBINDING SITE FOR RESIDUE MG A 2000
ChainResidue
AASN38
AADP1000
AHOH3001
AHOH3002
AHOH3003

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ADP A 1000
ChainResidue
AHIS93
ALYS99
ALYS103
AGLY126
APHE127
ATHR174
AMG2000
AHOH3001
AHOH3002
AHOH3003
AHOH3004
AHOH3006
AHOH3007
AHOH3009
AHOH3067
AHOH3101
AHOH3134
AHOH3212
AHOH3214
AASN38
AALA42
AASP80
AMET85

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HEZ A 4000
ChainResidue
APHE9
ALYS14
AASP44
AARG47
APHE48
ALEU51
AGLN122
AHOH3024
AHOH3042

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HEZ A 4001
ChainResidue
AGLN10
AARG33
AGLU34
ASER37
AGLY121
AGLY124

Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR25-GLU34

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15837196
ChainResidueDetails
AASN38
AASP80
APHE127
ATHR174

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PDB entries from 2025-06-11

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