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1JBE

1.08 A Structure of apo-Chey reveals meta-active conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000156molecular_functionphosphorelay response regulator activity
A0000160biological_processphosphorelay signal transduction system
A0000287molecular_functionmagnesium ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006935biological_processchemotaxis
A0007165biological_processsignal transduction
A0009288cellular_componentbacterial-type flagellum
A0009433cellular_componentbacterial-type flagellum basal body, C ring
A0009454biological_processaerotaxis
A0016407molecular_functionacetyltransferase activity
A0018393biological_processinternal peptidyl-lysine acetylation
A0043052biological_processthermotaxis
A0046872molecular_functionmetal ion binding
A0050920biological_processregulation of chemotaxis
A0071977biological_processbacterial-type flagellum-dependent swimming motility
A0097588biological_processarchaeal or bacterial-type flagellum-dependent cell motility
A0120107cellular_componentbacterial-type flagellum rotor complex
A1902021biological_processregulation of bacterial-type flagellum-dependent cell motility
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AASN59
ALYS109
AGOL201
AHOH411
AHOH416
AHOH460

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
ATYR106
ALYS119
ALYS122
AHOH424
AHOH428
AHOH441
AHOH448
AHOH451
APRO61
AASN62
AGLY105

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AASP13
APHE14
ASER15
AALA74
ASNN75
AGLY76
AGLN100
AGOL202
AHOH410
AHOH528
AHOH549
AHOH551

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 201
ChainResidue
AASP12
APHE14
AMET17
AGLN47
ALYS109
ASO4301
AHOH457
AHOH460
AHOH537

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 202
ChainResidue
AASP13
ASER15
AARG18
AGLU37
ASO4303
AHOH414

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A0A0H3AMJ9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8176739","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CHN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"4-aspartylphosphate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1869568","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2689446","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"11359578","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9560203","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"1390767","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9560203","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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