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4I5O

Crystal Structure of W-W-R ClpX Hexamer

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
D0005524molecular_functionATP binding
D0006457biological_processprotein folding
D0016887molecular_functionATP hydrolysis activity
D0051082molecular_functionunfolded protein binding
D0140662molecular_functionATP-dependent protein folding chaperone
E0005524molecular_functionATP binding
E0006457biological_processprotein folding
E0016887molecular_functionATP hydrolysis activity
E0051082molecular_functionunfolded protein binding
E0140662molecular_functionATP-dependent protein folding chaperone
F0005524molecular_functionATP binding
F0006457biological_processprotein folding
F0016887molecular_functionATP hydrolysis activity
F0051082molecular_functionunfolded protein binding
F0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AGLY122
ASER123
AGLY124
ALYS125
ATHR126

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
BLYS125
BTHR126
BPRO120
BGLY122
BSER123
BGLY124

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C 501
ChainResidue
CPRO120
CTHR121
CGLY122
CSER123
CGLY124
CLYS125
CTHR126
CTYR182

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 501
ChainResidue
DGLY122
DSER123
DGLY124
DLYS125
DTHR126

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 E 501
ChainResidue
EGLY122
ESER123
EGLY124
ELYS125
ETHR126

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 F 501
ChainResidue
FPRO120
FGLY122
FSER123
FGLY124
FLYS125
FTHR126

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00175, ECO:0000269|PubMed:19914167, ECO:0000269|PubMed:23622246
ChainResidueDetails
APRO120
BPRO120
CPRO120
DPRO120
EPRO120
FPRO120

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PDB entries from 2024-05-01

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