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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1U8T

Crystal structure of CheY D13K Y106W alone and in complex with a FliM peptide

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
B0000156molecular_functionphosphorelay response regulator activity
B0000160biological_processphosphorelay signal transduction system
B0000287molecular_functionmagnesium ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006935biological_processchemotaxis
B0007165biological_processsignal transduction
B0009288cellular_componentbacterial-type flagellum
B0009433cellular_componentbacterial-type flagellum basal body, C ring
B0009454biological_processaerotaxis
B0016407molecular_functionacetyltransferase activity
B0018393biological_processinternal peptidyl-lysine acetylation
B0043052biological_processthermotaxis
B0046872molecular_functionmetal ion binding
B0050920biological_processregulation of chemotaxis
B0071977biological_processbacterial-type flagellum-dependent swimming motility
B0097588biological_processarchaeal or bacterial-type flagellum-dependent cell motility
B0120107cellular_componentbacterial-type flagellum rotor complex
B1902021biological_processregulation of bacterial-type flagellum-dependent cell motility
C0000156molecular_functionphosphorelay response regulator activity
C0000160biological_processphosphorelay signal transduction system
C0000287molecular_functionmagnesium ion binding
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006935biological_processchemotaxis
C0007165biological_processsignal transduction
C0009288cellular_componentbacterial-type flagellum
C0009433cellular_componentbacterial-type flagellum basal body, C ring
C0009454biological_processaerotaxis
C0016407molecular_functionacetyltransferase activity
C0018393biological_processinternal peptidyl-lysine acetylation
C0043052biological_processthermotaxis
C0046872molecular_functionmetal ion binding
C0050920biological_processregulation of chemotaxis
C0071977biological_processbacterial-type flagellum-dependent swimming motility
C0097588biological_processarchaeal or bacterial-type flagellum-dependent cell motility
C0120107cellular_componentbacterial-type flagellum rotor complex
C1902021biological_processregulation of bacterial-type flagellum-dependent cell motility
D0000156molecular_functionphosphorelay response regulator activity
D0000160biological_processphosphorelay signal transduction system
D0000287molecular_functionmagnesium ion binding
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006935biological_processchemotaxis
D0007165biological_processsignal transduction
D0009288cellular_componentbacterial-type flagellum
D0009433cellular_componentbacterial-type flagellum basal body, C ring
D0009454biological_processaerotaxis
D0016407molecular_functionacetyltransferase activity
D0018393biological_processinternal peptidyl-lysine acetylation
D0043052biological_processthermotaxis
D0046872molecular_functionmetal ion binding
D0050920biological_processregulation of chemotaxis
D0071977biological_processbacterial-type flagellum-dependent swimming motility
D0097588biological_processarchaeal or bacterial-type flagellum-dependent cell motility
D0120107cellular_componentbacterial-type flagellum rotor complex
D1902021biological_processregulation of bacterial-type flagellum-dependent cell motility
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 601
ChainResidue
CLYS7
CASN32
CHOH653
CHOH656
CHOH719
DARG22
DLYS26
site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 C 602
ChainResidue
CHOH637
CHOH652
CHOH716
DGLU5
DLYS7
DASN32
DHOH707
CARG22
CLYS26
site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 603
ChainResidue
CVAL107
CVAL108
CTHR115
CLYS119
CHOH633
site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 604
ChainResidue
DTRP106
DVAL107
DVAL108
DLYS119
DHOH631
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A0A0H3AMJ9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8176739","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CHN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
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 Residues4
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 Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"1390767","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9560203","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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