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1BDJ

COMPLEX STRUCTURE OF HPT DOMAIN AND CHEY

Functional Information from GO Data
ChainGOidnamespacecontents
A0000155molecular_functionphosphorelay sensor kinase activity
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
A0009927molecular_functionhistidine phosphotransfer kinase activity
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
B0000160biological_processphosphorelay signal transduction system
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 400
ChainResidue
AASP57
ATRP58
AASN59
ATHR87
AALA88
ALYS109

site_idPHA
Number of Residues1
DetailsPHOSPHO-ACCEPTOR RESIDUE.
ChainResidue
AASP57

site_idPHD
Number of Residues1
DetailsPHOSPHO-DONOR RESIDUE.
ChainResidue
BHIS715

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphohistidine => ECO:0000305|PubMed:10851007
ChainResidueDetails
BILE717

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN
ChainResidueDetails
APHE14
ATRP58
AMET60

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1869568, ECO:0000269|PubMed:2689446
ChainResidueDetails
ATRP58

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:11359578, ECO:0000269|PubMed:9560203
ChainResidueDetails
AGLU93

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:1390767, ECO:0000269|PubMed:9560203
ChainResidueDetails
APRO110

218853

PDB entries from 2024-04-24

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