3BZM

Crystal Structure of Open form of Menaquinone-Specific Isochorismate Synthase, MenF

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0008909	molecular_function	isochorismate synthase activity
A	0009058	biological_process	biosynthetic process
A	0009234	biological_process	menaquinone biosynthetic process
A	0016853	molecular_function	isomerase activity
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CIT A 432

Chain	Residue
A	GLN57
A	ARG58
A	ASN59
A	ARG241
A	ARG244
A	ARG251
A	HOH520

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01935, ECO:0000269|PubMed:17240978

Chain	Residue	Details
A	LYS190

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01935, ECO:0000269|PubMed:17240978

Chain	Residue	Details
A	GLU240

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01935, ECO:0000269|PubMed:18453696

Chain	Residue	Details
A	GLU284
A	GLU416

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1i7q

Chain	Residue	Details
A	HIS318

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 325

Chain	Residue	Details
A	LYS190	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLU240	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLU284	attractive charge-charge interaction, electrostatic stabiliser, metal ligand
A	GLU416	attractive charge-charge interaction, electrostatic stabiliser, metal ligand
A	LYS420	attractive charge-charge interaction, electrostatic stabiliser

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