1SPH

REFINED STRUCTURES OF THE ACTIVE S83C AND IMPAIRED S46D HPRS: EVIDENCE THAT PHOSPHORYLATION DOES NOT REQUIRE A BACKBONE CONFORMATIONAL TRANSITION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0009401	biological_process	phosphoenolpyruvate-dependent sugar phosphotransferase system
A	0043610	biological_process	regulation of carbohydrate utilization
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0009401	biological_process	phosphoenolpyruvate-dependent sugar phosphotransferase system
B	0043610	biological_process	regulation of carbohydrate utilization

Functional Information from PDB Data

site_id	ACA
Number of Residues	1
Details	ACTIVE SITE HISTIDINE IN CHAIN A

Chain	Residue
A	HIS15

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site_id	ACB
Number of Residues	1
Details	ACTIVE SITE HISTIDINE IN CHAIN B

Chain	Residue
B	HIS15

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Functional Information from PROSITE/UniProt

site_id	PS00369
Number of Residues	8
Details	PTS_HPR_HIS PTS HPR domain histidine phosphorylation site signature. GIHARPAT

Chain	Residue	Details
A	GLY13-THR20

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Pros-phosphohistidine intermediate; alternate => ECO:0000255|PROSITE-ProRule:PRU00681, ECO:0000269|PubMed:1549615

Chain	Residue	Details
A	ALA16
B	ALA16

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site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:17218307

Chain	Residue	Details
A	GLY13
B	GLY13

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Tele-phosphohistidine; alternate => ECO:0000269|PubMed:1549615

Chain	Residue	Details
A	ALA16
B	ALA16

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine; by HPrK/P => ECO:0000255|PROSITE-ProRule:PRU00681, ECO:0000269|PubMed:17218307

Chain	Residue	Details
A	ILE47
B	ILE47

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