Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1A0O

CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000156	molecular_function	phosphorelay response regulator activity
A	0000160	biological_process	phosphorelay signal transduction system
A	0000287	molecular_function	magnesium ion binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006935	biological_process	chemotaxis
A	0007165	biological_process	signal transduction
A	0009288	cellular_component	bacterial-type flagellum
A	0009433	cellular_component	bacterial-type flagellum basal body, C ring
A	0009454	biological_process	aerotaxis
A	0016407	molecular_function	acetyltransferase activity
A	0018393	biological_process	internal peptidyl-lysine acetylation
A	0043052	biological_process	thermotaxis
A	0046872	molecular_function	metal ion binding
A	0050920	biological_process	regulation of chemotaxis
A	0071977	biological_process	bacterial-type flagellum-dependent swimming motility
A	0097588	biological_process	archaeal or bacterial-type flagellum-dependent cell motility
A	0120107	cellular_component	bacterial-type flagellum rotor complex
A	1902021	biological_process	regulation of bacterial-type flagellum-dependent cell motility
C	0000156	molecular_function	phosphorelay response regulator activity
C	0000160	biological_process	phosphorelay signal transduction system
C	0000287	molecular_function	magnesium ion binding
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006935	biological_process	chemotaxis
C	0007165	biological_process	signal transduction
C	0009288	cellular_component	bacterial-type flagellum
C	0009433	cellular_component	bacterial-type flagellum basal body, C ring
C	0009454	biological_process	aerotaxis
C	0016407	molecular_function	acetyltransferase activity
C	0018393	biological_process	internal peptidyl-lysine acetylation
C	0043052	biological_process	thermotaxis
C	0046872	molecular_function	metal ion binding
C	0050920	biological_process	regulation of chemotaxis
C	0071977	biological_process	bacterial-type flagellum-dependent swimming motility
C	0097588	biological_process	archaeal or bacterial-type flagellum-dependent cell motility
C	0120107	cellular_component	bacterial-type flagellum rotor complex
C	1902021	biological_process	regulation of bacterial-type flagellum-dependent cell motility
E	0000156	molecular_function	phosphorelay response regulator activity
E	0000160	biological_process	phosphorelay signal transduction system
E	0000287	molecular_function	magnesium ion binding
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006935	biological_process	chemotaxis
E	0007165	biological_process	signal transduction
E	0009288	cellular_component	bacterial-type flagellum
E	0009433	cellular_component	bacterial-type flagellum basal body, C ring
E	0009454	biological_process	aerotaxis
E	0016407	molecular_function	acetyltransferase activity
E	0018393	biological_process	internal peptidyl-lysine acetylation
E	0043052	biological_process	thermotaxis
E	0046872	molecular_function	metal ion binding
E	0050920	biological_process	regulation of chemotaxis
E	0071977	biological_process	bacterial-type flagellum-dependent swimming motility
E	0097588	biological_process	archaeal or bacterial-type flagellum-dependent cell motility
E	0120107	cellular_component	bacterial-type flagellum rotor complex
E	1902021	biological_process	regulation of bacterial-type flagellum-dependent cell motility
G	0000156	molecular_function	phosphorelay response regulator activity
G	0000160	biological_process	phosphorelay signal transduction system
G	0000287	molecular_function	magnesium ion binding
G	0005515	molecular_function	protein binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006935	biological_process	chemotaxis
G	0007165	biological_process	signal transduction
G	0009288	cellular_component	bacterial-type flagellum
G	0009433	cellular_component	bacterial-type flagellum basal body, C ring
G	0009454	biological_process	aerotaxis
G	0016407	molecular_function	acetyltransferase activity
G	0018393	biological_process	internal peptidyl-lysine acetylation
G	0043052	biological_process	thermotaxis
G	0046872	molecular_function	metal ion binding
G	0050920	biological_process	regulation of chemotaxis
G	0071977	biological_process	bacterial-type flagellum-dependent swimming motility
G	0097588	biological_process	archaeal or bacterial-type flagellum-dependent cell motility
G	0120107	cellular_component	bacterial-type flagellum rotor complex
G	1902021	biological_process	regulation of bacterial-type flagellum-dependent cell motility

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN C 1

Chain	Residue
C	ASP13
C	ASP57
C	ASN59

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN G 130

Chain	Residue
G	ASP13
G	ASP57
G	ASN59

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN E 130

Chain	Residue
E	ASN59
E	ASP12
E	ASP13
E	ASP57

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN A 130

Chain	Residue
A	ASP13
A	ASP57
A	ASN59

Functional Information from PROSITE/UniProt

site_id	PS00430
Number of Residues	108
Details	TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. rqlaleakgetpsavtrlsvvaksepqdeqsrsqsprriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfvieadqitf...............ETVEVSPK

Chain	Residue	Details
B	ARG124-LYS231

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	468
Details	Domain: {"description":"Response regulatory","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0H3AMJ9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8176739","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CHN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"11359578","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9560203","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"1390767","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9560203","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)