1I2L

DEOXYCHORISMATE LYASE FROM ESCHERICHIA COLI WITH INHIBITOR

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	17
Details	BINDING SITE FOR RESIDUE DCS A 301

Chain	Residue
A	ARG45
A	VAL197
A	GLY199
A	ILE200
A	MET201
A	ASN236
A	ALA237
A	HOH413
A	HOH577
A	TYR92
A	LYS140
A	GLN147
A	GLU173
A	CYS175
A	ALA176
A	ALA177
A	ASN178

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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	GLU173-ARG202

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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	LYS140

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 305

Chain	Residue	Details
A	THR28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	LYS140	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
A	GLU173	electrostatic stabiliser, hydrogen bond acceptor

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