4A29

Structure of the engineered retro-aldolase RA95.0

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	0016831	molecular_function	carboxy-lyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 3NK A 299

Chain	Residue
A	MET180
A	ARG182
A	ASP183
A	GLY187
A	LYS210
A	MLT300
A	HOH2303
A	HOH2340

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site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE MLT A 300

Chain	Residue
A	SER56
A	SER58
A	PHE89
A	ARG182
A	GLY212
A	SER233
A	SER234
A	3NK299
A	HOH2160
A	HOH2175
A	HOH2304
A	GLU53

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 252

Chain	Residue	Details
A	VAL51	electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity, proton acceptor, proton donor
A	GLU53	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
A	SER110	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	LEU159	activator, hydrogen bond acceptor, increase nucleophilicity
A	MET180	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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