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5OG1

Cryo EM structure of the E. coli disaggregase ClpB (BAP form, DWB mutant), in the ATPgammaS state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0009408biological_processresponse to heat
A0016887molecular_functionATP hydrolysis activity
A0042026biological_processprotein refolding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0009408biological_processresponse to heat
B0016887molecular_functionATP hydrolysis activity
B0042026biological_processprotein refolding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0009408biological_processresponse to heat
C0016887molecular_functionATP hydrolysis activity
C0042026biological_processprotein refolding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0009408biological_processresponse to heat
D0016887molecular_functionATP hydrolysis activity
D0042026biological_processprotein refolding
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0009408biological_processresponse to heat
E0016887molecular_functionATP hydrolysis activity
E0042026biological_processprotein refolding
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0009408biological_processresponse to heat
F0016887molecular_functionATP hydrolysis activity
F0042026biological_processprotein refolding
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue AGS C 901
ChainResidue
BARG332
CTHR315
CILE349
CLEU353
CTYR357
CILE391
CASP178
CPRO179
CVAL180
CGLY209
CGLY211
CLYS212
CTHR213
CALA214

site_idAC2
Number of Residues12
Detailsbinding site for residue AGS C 902
ChainResidue
BASP593
BLEU691
BASP695
BASP696
BGLU752
BARG756
CGLY610
CLYS611
CTHR612
CGLU613
CARG631
CARG815

site_idAC3
Number of Residues12
Detailsbinding site for residue AGS E 901
ChainResidue
EARG183
EGLY209
EVAL210
EGLY211
ELYS212
ETHR213
EALA214
EASP278
EALA313
EILE349
EPRO387
EASP388

site_idAC4
Number of Residues12
Detailsbinding site for residue AGS E 902
ChainResidue
DASP696
EARG569
EGLY610
ELYS611
ETHR612
EGLU613
EARG631
EASP677
ETHR717
EASN719
EGLN778
EARG815

site_idAC5
Number of Residues10
Detailsbinding site for residue AGS D 901
ChainResidue
CALA328
DPRO208
DGLY209
DVAL210
DGLY211
DLYS212
DTHR213
DPRO387
DASP388
DILE391

site_idAC6
Number of Residues11
Detailsbinding site for residue AGS D 902
ChainResidue
CLEU691
CASP695
CARG750
CGLU752
DVAL609
DGLY610
DLYS611
DTHR612
DGLU613
DLYS616
DARG631

site_idAC7
Number of Residues14
Detailsbinding site for residue AGS B 901
ChainResidue
AALA327
AARG331
BPRO179
BARG183
BGLU207
BPRO208
BVAL210
BGLY211
BTHR213
BALA214
BLEU353
BTYR357
BASP388
BILE391

Functional Information from PROSITE/UniProt
site_idPS00870
Number of Residues13
DetailsCLPAB_1 Chaperonins clpA/B signature 1. DAGNMLKPaLarG
ChainResidueDetails
CASP294-GLY306

site_idPS00871
Number of Residues19
DetailsCLPAB_2 Chaperonins clpA/B signature 2. RIDmSEFmEKhSvSRLvGA
ChainResidueDetails
CARG631-ALA649

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues84
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1260
DetailsRegion: {"description":"NBD2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues546
DetailsRegion: {"description":"C-terminal"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues13
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues612
DetailsRegion: {"description":"Linker"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues402
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues65
DetailsRegion: {"description":"Repeat 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01251","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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