4A2R

Structure of the engineered retro-aldolase RA95.5-5

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000162	biological_process	L-tryptophan biosynthetic process
A	0004425	molecular_function	indole-3-glycerol-phosphate synthase activity
A	0006568	biological_process	L-tryptophan metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0009073	biological_process	aromatic amino acid family biosynthetic process
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 3NK A 1083

Chain	Residue
A	LYS83
A	MET182
A	PHE184
A	HOH2104
A	PHE89
A	ASN110
A	ASP111
A	PHE112
A	ILE133
A	LYS135
A	ASN161
A	PHE180

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 252

Chain	Residue	Details
A	TYR51	electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity, proton acceptor, proton donor
A	THR53	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
A	ASN110	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	LEU159	activator, hydrogen bond acceptor, increase nucleophilicity
A	PHE180	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity
A	LYS210	electrostatic stabiliser
A	LEU211	electrostatic stabiliser, hydrogen bond donor

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