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5OFO

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

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 Residues12
Detailsbinding site for residue AGS C 901
ChainResidue
BARG332
CALA214
CILE349
CPRO387
CVAL180
CGLU207
CPRO208
CGLY209
CVAL210
CGLY211
CLYS212
CTHR213

site_idAC2
Number of Residues12
Detailsbinding site for residue AGS C 902
ChainResidue
BGLU752
BARG756
CARG569
CILE571
CGLY608
CVAL609
CGLY610
CLYS611
CTHR612
CGLU613
CALA814
CARG815

site_idAC3
Number of Residues17
Detailsbinding site for residue AGS F 901
ChainResidue
EALA327
EGLU330
EARG331
FPRO179
FVAL180
FILE181
FARG183
FGLU207
FPRO208
FGLY209
FVAL210
FGLY211
FLYS212
FTHR213
FALA214
FILE349
FPRO387

site_idAC4
Number of Residues11
Detailsbinding site for residue AGS F 902
ChainResidue
FTHR607
FGLY608
FVAL609
FGLY610
FLYS611
FTHR612
FGLU613
FARG631
FLEU766
FILE774
FARG815

site_idAC5
Number of Residues11
Detailsbinding site for residue AGS E 901
ChainResidue
DARG331
EILE181
EGLY209
EVAL210
EGLY211
ELYS212
ETHR213
EALA214
EASP278
EILE349
ELEU353

site_idAC6
Number of Residues11
Detailsbinding site for residue AGS E 902
ChainResidue
DGLU752
EARG569
ETHR607
EGLY608
EVAL609
EGLY610
ELYS611
ETHR612
EGLU613
EASN719
EARG815

site_idAC7
Number of Residues14
Detailsbinding site for residue AGS D 901
ChainResidue
CARG331
CARG332
DPRO179
DARG183
DGLU207
DGLY209
DVAL210
DGLY211
DLYS212
DTHR213
DALA214
DILE349
DPRO387
DASP388

site_idAC8
Number of Residues12
Detailsbinding site for residue AGS D 902
ChainResidue
DILE774
CASP695
CARG750
CGLU752
DILE571
DTHR607
DGLY608
DVAL609
DGLY610
DLYS611
DTHR612
DGLU613

site_idAC9
Number of Residues12
Detailsbinding site for residue AGS B 901
ChainResidue
AARG331
AARG332
BVAL180
BGLU207
BPRO208
BVAL210
BGLY211
BLYS212
BTHR213
BALA214
BILE349
BPRO387

site_idAD1
Number of Residues11
Detailsbinding site for residue AGS B 902
ChainResidue
BARG569
BGLY608
BVAL609
BGLY610
BLYS611
BTHR612
BGLU613
BASN719
BILE774
BALA814
BARG815

site_idAD2
Number of Residues14
Detailsbinding site for residue AGS A 901
ChainResidue
AASP178
AVAL180
AILE181
AARG183
AGLY209
AVAL210
AGLY211
ALYS212
ATHR213
AALA214
AILE349
ALEU353
APRO387
FARG331

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 Residues12
DetailsBINDING:
ChainResidueDetails
CGLY206
BGLY605
AGLY206
AGLY605
CGLY605
FGLY206
FGLY605
EGLY206
EGLY605
DGLY206
DGLY605
BGLY206

site_idSWS_FT_FI2
Number of Residues18
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
CLYS96
DLYS96
DLYS176
DLYS640
BLYS96
BLYS176
BLYS640
ALYS96
ALYS176
ALYS640
CLYS176
CLYS640
FLYS96
FLYS176
FLYS640
ELYS96
ELYS176
ELYS640

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PDB entries from 2024-07-17

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