8ZLV

Asymmetric Dimeric Structure of the Catalytic Domain in Truncated Threonine Deaminase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004794	molecular_function	threonine deaminase activity
A	0006520	biological_process	amino acid metabolic process
A	0009097	biological_process	isoleucine biosynthetic process
A	0030170	molecular_function	pyridoxal phosphate binding
B	0004794	molecular_function	threonine deaminase activity
B	0006520	biological_process	amino acid metabolic process
B	0009097	biological_process	isoleucine biosynthetic process
B	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	6
Details	BINDING: BINDING => ECO:0000269|PubMed:9562556

Chain	Residue	Details
A	ASN89
A	GLY188
A	SER315
B	ASN89
B	GLY188
B	SER315

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site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:9562556

Chain	Residue	Details
A	LLP62
B	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	SER315	electrostatic stabiliser

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site_id	MCSA2
Number of Residues	2
Details	M-CSA 886

Chain	Residue	Details
B	LLP62	covalent catalysis, proton shuttle (general acid/base)
B	SER315	electrostatic stabiliser

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