7M3S

The internal aldimine form of the wild-type Salmonella Typhimurium Tryptophan Synthase in complex with N-(4'-trifluoromethoxybenzoyl)-2-amino-1-ethylphosphate (F6F) inhibitor at the alpha-and beta-site, sodium ion at the metal coordination site, and another F6F molecule at the enzyme beta-site at 1.55 Angstrom resolution. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000162	biological_process	tryptophan biosynthetic process
A	0004834	molecular_function	tryptophan synthase activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006568	biological_process	tryptophan metabolic process
A	0016829	molecular_function	lyase activity
B	0000162	biological_process	tryptophan biosynthetic process
B	0004834	molecular_function	tryptophan synthase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0006568	biological_process	tryptophan metabolic process
B	0016829	molecular_function	lyase activity
B	0042802	molecular_function	identical protein binding

Functional Information from PROSITE/UniProt

site_id	PS00167
Number of Residues	14
Details	TRP_SYNTHASE_ALPHA Tryptophan synthase alpha chain signature. LELGvPFSDPLADG

Chain	Residue	Details
A	LEU48-GLY61

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site_id	PS00168
Number of Residues	15
Details	TRP_SYNTHASE_BETA Tryptophan synthase beta chain pyridoxal-phosphate attachment site. LlHgGAHKtNqvLgQ

Chain	Residue	Details
B	LEU80-GLN94

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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
B	LYS87
A	ASP60

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 383

Chain	Residue	Details
B	LYS87	electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
B	GLU109
B	SER377	hydrogen bond donor

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