6VU0

CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF ENZYME I OF THE BACTERIAL PHOSPHOTRANSFERASE SYSTEM FROM THE ESCHERICHIA COLI ENZYME

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0016310	biological_process	phosphorylation
A	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
B	0003824	molecular_function	catalytic activity
B	0016310	biological_process	phosphorylation
B	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue SO4 A 600

Chain	Residue
A	ARG296
A	ARG332

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site_id	AC2
Number of Residues	3
Details	binding site for residue SO4 B 601

Chain	Residue
B	ARG296
B	ARG332
B	ASN454

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Functional Information from PROSITE/UniProt

site_id	PS00742
Number of Residues	19
Details	PEP_ENZYMES_2 PEP-utilizing enzymes signature 2. DfFSIGTNDLtQYTLAvdR

Chain	Residue	Details
A	ASP447-ARG465

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:12705838, ECO:0000305|PubMed:17053069

Chain	Residue	Details
A	CYS502
B	CYS502

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P23533

Chain	Residue	Details
A	ARG296
A	ARG465
B	ARG296
B	ARG465

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site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:17053069

Chain	Residue	Details
A	ARG332
A	GLU431
A	ASN454
A	ASP455
B	ARG332
B	GLU431
B	ASN454
B	ASP455

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 920

Chain	Residue	Details
A	GLU431	metal ligand
A	ASP455	metal ligand
A	CYS502	proton shuttle (general acid/base)

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site_id	MCSA2
Number of Residues	3
Details	M-CSA 920

Chain	Residue	Details
B	GLU431	metal ligand
B	ASP455	metal ligand
B	CYS502	proton shuttle (general acid/base)

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