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CRYSTAL STRUCTURE OF AMINODEOXYCHORISMATE LYASE FROM ESCHERICHIA COLI

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005829	cellular_component	cytosol
A	0008153	biological_process	para-aminobenzoic acid biosynthetic process
A	0008696	molecular_function	4-amino-4-deoxychorismate lyase activity
A	0016829	molecular_function	lyase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0046394	biological_process	carboxylic acid biosynthetic process
A	0046654	biological_process	tetrahydrofolate biosynthetic process
A	0046656	biological_process	folic acid biosynthetic process
A	1901566	biological_process	organonitrogen compound biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP A 413

Chain	Residue
A	ARG59
A	MET221
A	ASN256
A	ALA257
A	HOH529
A	HOH546
A	TYR109
A	LYS159
A	GLU193
A	CYS195
A	ALA196
A	ALA197
A	GLY219
A	ILE220

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Functional Information from PROSITE/UniProt

site_id	PS00770
Number of Residues	30
Details	AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EcCaaNLFwrkgnv......VyTprldqag.VnGImR

Chain	Residue	Details
A	GLU193-ARG222

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine

Chain	Residue	Details
A	LYS159

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 305

Chain	Residue	Details
A	THR38	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	LYS159	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
A	GLU193	electrostatic stabiliser, hydrogen bond acceptor

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