7RNQ

Holo structure of engineered TrpB, 2B9-H275E, from Pyrococcus furiosus in the extended-open conformation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000162	biological_process	tryptophan biosynthetic process
A	0004834	molecular_function	tryptophan synthase activity
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	0006568	biological_process	tryptophan metabolic process
B	0016829	molecular_function	lyase activity
C	0000162	biological_process	tryptophan biosynthetic process
C	0004834	molecular_function	tryptophan synthase activity
C	0006568	biological_process	tryptophan metabolic process
C	0016829	molecular_function	lyase activity
D	0000162	biological_process	tryptophan biosynthetic process
D	0004834	molecular_function	tryptophan synthase activity
D	0006568	biological_process	tryptophan metabolic process
D	0016829	molecular_function	lyase activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU75-GLN89

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250

Chain	Residue	Details
A	LLP82
B	LLP82
C	LLP82
D	LLP82

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