1VE5

Crystal Structure of T.th. HB8 Threonine deaminase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0003941	molecular_function	L-serine ammonia-lyase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006520	biological_process	amino acid metabolic process
A	0008721	molecular_function	D-serine ammonia-lyase activity
A	0018114	molecular_function	threonine racemase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0030378	molecular_function	serine racemase activity
A	0046872	molecular_function	metal ion binding
A	0070179	biological_process	D-serine biosynthetic process
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0003941	molecular_function	L-serine ammonia-lyase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006520	biological_process	amino acid metabolic process
B	0008721	molecular_function	D-serine ammonia-lyase activity
B	0018114	molecular_function	threonine racemase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0030378	molecular_function	serine racemase activity
B	0046872	molecular_function	metal ion binding
B	0070179	biological_process	D-serine biosynthetic process
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0003941	molecular_function	L-serine ammonia-lyase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006520	biological_process	amino acid metabolic process
C	0008721	molecular_function	D-serine ammonia-lyase activity
C	0018114	molecular_function	threonine racemase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0030378	molecular_function	serine racemase activity
C	0046872	molecular_function	metal ion binding
C	0070179	biological_process	D-serine biosynthetic process
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0003941	molecular_function	L-serine ammonia-lyase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006520	biological_process	amino acid metabolic process
D	0008721	molecular_function	D-serine ammonia-lyase activity
D	0018114	molecular_function	threonine racemase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0030378	molecular_function	serine racemase activity
D	0046872	molecular_function	metal ion binding
D	0070179	biological_process	D-serine biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 2001

Chain	Residue
A	GLU203
A	ALA207
A	ASP209
A	HOH1067
A	HOH1223
A	HOH1231

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA D 2002

Chain	Residue
D	GLU203
D	ALA207
D	ASP209

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 2003

Chain	Residue
B	GLU203
B	ALA207
B	ASP209
B	HOH1012

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA C 2004

Chain	Residue
C	GLU203
C	ALA207
C	ASP209
C	HOH1063

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site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP A 413

Chain	Residue
A	PHE50
A	LYS51
A	ASN75
A	PRO176
A	GLY178
A	GLY179
A	GLY180
A	GLY181
A	LEU182
A	GLU277
A	THR279
A	SER303
A	GLY304
A	HOH1019
A	HOH1109
A	HOH1175

---

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP B 913

Chain	Residue
B	PHE50
B	LYS51
B	ASN75
B	PRO176
B	VAL177
B	GLY178
B	GLY179
B	GLY180
B	GLY181
B	LEU182
B	GLU277
B	THR279
B	SER303
B	HOH1001
B	HOH1129

---

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP C 1413

Chain	Residue
C	PHE50
C	LYS51
C	ASN75
C	PRO176
C	GLY178
C	GLY179
C	GLY180
C	GLY181
C	LEU182
C	GLU277
C	THR279
C	SER303
C	HOH1039
C	HOH1043

---

site_id	AC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP D 1913

Chain	Residue
D	PHE50
D	LYS51
D	ASN75
D	PRO176
D	GLY178
D	GLY179
D	GLY180
D	GLY181
D	LEU182
D	VAL233
D	GLU277
D	THR279
D	SER303
D	GLY304
D	HOH1008
D	HOH1011
D	HOH1234

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLU42-ALA55

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