9D2Q

Crystal structure of E. coli Threonine dehydratase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004794	molecular_function	threonine deaminase activity
A	0006566	biological_process	threonine metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0009066	biological_process	aspartate family amino acid metabolic process
A	0009082	biological_process	branched-chain amino acid biosynthetic process
A	0009097	biological_process	isoleucine biosynthetic process
A	0016597	molecular_function	amino acid binding
A	0016829	molecular_function	lyase activity
A	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PROSITE/UniProt

site_id	PS00165
Number of Residues	14
Details	DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Edrqp.VHSFKLRGA

Chain	Residue	Details
A	GLU53-ALA66

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:9562556

Chain	Residue	Details
A	ASN89
A	GLY188
A	SER315

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:9562556

Chain	Residue	Details
A	LLP62

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 886

Chain	Residue	Details
A	LLP62	covalent catalysis, proton shuttle (general acid/base)
A	VAL319	electrostatic stabiliser

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