8ZKV

Engineering Threonine Deaminase Catalytic Domain into a Tetrameric Configuration, Independent of Allosteric Regulation

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	12
Details	BINDING: BINDING => ECO:0000269|PubMed:9562556

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

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site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:9562556

Chain	Residue	Details
A	LLP62
B	LLP62
C	LLP62
D	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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site_id	MCSA3
Number of Residues	2
Details	M-CSA 886

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

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site_id	MCSA4
Number of Residues	2
Details	M-CSA 886

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

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