3OO1

Structure of E. Coli CheY mutant A113P in the absence of Sulfate

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
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	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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 130

Chain	Residue
A	ASP13
A	ASP57
A	ASN59
A	HOH173
A	HOH212
A	HOH262
A	HOH352

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG B 130

Chain	Residue
B	ASP57
B	ASN59
B	HOH136
B	HOH155
B	HOH165
B	ASP12
B	ASP13

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:A0A0H3AMJ9

Chain	Residue	Details
A	ASP12
B	ASP12

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN

Chain	Residue	Details
A	ASP13
A	ASP57
A	ASN59
B	ASP13
B	ASP57
B	ASN59

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1869568, ECO:0000269|PubMed:2689446

Chain	Residue	Details
A	ASP57
B	ASP57

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:11359578, ECO:0000269|PubMed:9560203

Chain	Residue	Details
A	LYS92
B	LYS92

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:1390767, ECO:0000269|PubMed:9560203

Chain	Residue	Details
A	LYS109
B	LYS109

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