Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1F4V

CRYSTAL STRUCTURE OF ACTIVATED CHEY BOUND TO THE N-TERMINUS OF FLIM

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000155	molecular_function	phosphorelay sensor kinase activity
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	0009927	molecular_function	histidine phosphotransfer kinase activity
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
B	0000155	molecular_function	phosphorelay sensor kinase activity
B	0000156	molecular_function	phosphorelay response regulator activity
B	0000160	biological_process	phosphorelay signal transduction system
B	0000287	molecular_function	magnesium ion binding
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006935	biological_process	chemotaxis
B	0007165	biological_process	signal transduction
B	0009288	cellular_component	bacterial-type flagellum
B	0009433	cellular_component	bacterial-type flagellum basal body, C ring
B	0009454	biological_process	aerotaxis
B	0009927	molecular_function	histidine phosphotransfer kinase activity
B	0016407	molecular_function	acetyltransferase activity
B	0018393	biological_process	internal peptidyl-lysine acetylation
B	0043052	biological_process	thermotaxis
B	0046872	molecular_function	metal ion binding
B	0050920	biological_process	regulation of chemotaxis
B	0071977	biological_process	bacterial-type flagellum-dependent swimming motility
B	0097588	biological_process	archaeal or bacterial-type flagellum-dependent cell motility
B	0120107	cellular_component	bacterial-type flagellum rotor complex
B	1902021	biological_process	regulation of bacterial-type flagellum-dependent cell motility
C	0000155	molecular_function	phosphorelay sensor kinase activity
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	0009927	molecular_function	histidine phosphotransfer kinase activity
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 301

Chain	Residue
B	ASP12
B	ASP13
B	ASP57
B	ASN59
B	BEF130
B	HOH324
B	HOH331

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 302

Chain	Residue
A	ASN59
A	BEF130
A	HOH416
A	HOH428
A	ASP13
A	ASP57

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG C 303

Chain	Residue
C	ASP13
C	PHE14
C	ASP57
C	ASN59
C	BEF130
C	HOH310
C	HOH333

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BEF A 130

Chain	Residue
A	ASP57
A	TRP58
A	ASN59
A	THR87
A	ALA88
A	LYS109
A	HOH383
B	MG302

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BEF B 130

Chain	Residue
A	LYS92
A	MET129
A	MG301
B	ASP57
B	TRP58
B	ASN59
B	THR87
B	ALA88
B	LYS109
B	HOH313

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BEF C 130

Chain	Residue
C	ASP57
C	TRP58
C	ASN59
C	THR87
C	ALA88
C	LYS109
C	MG303
C	HOH333

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 304

Chain	Residue
A	ARG19
A	LYS70
A	HOH391
A	HOH406

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 305

Chain	Residue
A	SER79
A	HOH340
B	ARG19
B	ARG22
B	HOH325
B	HOH389

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:A0A0H3AMJ9

Chain	Residue	Details
A	ASP13
B	ASP13
C	ASP13

site_id	SWS_FT_FI2
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269\|PubMed:8176739, ECO:0007744\|PDB:1CHN

Chain	Residue	Details
A	PHE14
A	TRP58
A	MET60
B	PHE14
B	TRP58
B	MET60
C	PHE14
C	TRP58
C	MET60

site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: 4-aspartylphosphate => ECO:0000255\|PROSITE-ProRule:PRU00169, ECO:0000269\|PubMed:1869568, ECO:0000269\|PubMed:2689446

Chain	Residue	Details
A	TRP58
B	TRP58
C	TRP58

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:11359578, ECO:0000269\|PubMed:9560203

Chain	Residue	Details
A	GLU93
B	GLU93
C	GLU93

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:1390767, ECO:0000269\|PubMed:9560203

Chain	Residue	Details
A	PRO110
B	PRO110
C	PRO110

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