Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6PP6

ClpX in ClpX-ClpP complex bound to substrate and ATP-gamma-S, class 3

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 Residues14
Detailsbinding site for residue AGS A 600
ChainResidue
ATHR121
AILE325
AALA369
AARG370
BGLU303
BARG307
AGLY122
ASER123
AGLY124
ALYS125
ATHR126
ALEU127
AASP184
AGLN185

site_idAC2
Number of Residues14
Detailsbinding site for residue AGS B 600
ChainResidue
BVAL78
BILE79
BPRO120
BGLY122
BSER123
BGLY124
BLYS125
BTHR126
BLEU127
BILE325
BALA369
BARG370
CGLU303
CARG307

site_idAC3
Number of Residues14
Detailsbinding site for residue AGS C 600
ChainResidue
CVAL78
CILE79
CPRO120
CGLY122
CSER123
CGLY124
CLYS125
CTHR126
CLEU127
CILE325
CALA369
CARG370
DGLU303
DARG307

site_idAC4
Number of Residues14
Detailsbinding site for residue AGS D 600
ChainResidue
DTYR77
DVAL78
DPRO120
DGLY122
DSER123
DGLY124
DLYS125
DTHR126
DLEU127
DGLN185
DILE325
DALA369
DARG370
EARG307

site_idAC5
Number of Residues10
Detailsbinding site for residue AGS E 600
ChainResidue
EILE79
EGLY122
ESER123
EGLY124
ELYS125
ETHR126
ELEU127
EILE325
EARG370
FARG307

site_idAC6
Number of Residues9
Detailsbinding site for residue ADP F 600
ChainResidue
FTHR121
FGLY122
FSER123
FGLY124
FLYS125
FTHR126
FLEU127
FILE325
FALA369

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

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon