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4CIU

Crystal structure of E. coli ClpB

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0009408biological_processresponse to heat
A0016887molecular_functionATP hydrolysis activity
A0042026biological_processprotein refolding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ADP A 901
ChainResidue
APRO179
ATHR213
AALA214
AILE349
APRO387
AASP388
AILE391
AVAL180
AILE181
AARG183
APRO208
AGLY209
AVAL210
AGLY211
ALYS212

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ADP A 902
ChainResidue
AARG569
AVAL570
AILE571
ATHR607
AGLY608
AVAL609
AGLY610
ALYS611
ATHR612
AGLU613
AILE774
AGLN778
AALA814
AARG815

Functional Information from PROSITE/UniProt
site_idPS00870
Number of Residues13
DetailsCLPAB_1 Chaperonins clpA/B signature 1. DAGNMLKPaLarG
ChainResidueDetails
AASP294-GLY306

site_idPS00871
Number of Residues19
DetailsCLPAB_2 Chaperonins clpA/B signature 2. RIDmSEFmEKhSvSRLvGA
ChainResidueDetails
AARG631-ALA649

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AGLY206
AGLY605

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS176
ALYS640

226707

PDB entries from 2024-10-30

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