2GN0

Crystal structure of dimeric biodegradative threonine deaminase (TdcB) from Salmonella typhimurium at 1.7 A resolution (Triclinic form with one complete subunit built in alternate conformation)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0003941	molecular_function	L-serine ammonia-lyase activity
A	0004794	molecular_function	threonine deaminase activity
A	0006520	biological_process	amino acid metabolic process
A	0006565	biological_process	L-serine catabolic process
A	0006567	biological_process	L-threonine catabolic process
A	0016829	molecular_function	lyase activity
A	0016841	molecular_function	ammonia-lyase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0070689	biological_process	L-threonine catabolic process to propionate
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0003941	molecular_function	L-serine ammonia-lyase activity
B	0004794	molecular_function	threonine deaminase activity
B	0006520	biological_process	amino acid metabolic process
B	0006565	biological_process	L-serine catabolic process
B	0006567	biological_process	L-threonine catabolic process
B	0016829	molecular_function	lyase activity
B	0016841	molecular_function	ammonia-lyase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0070689	biological_process	L-threonine catabolic process to propionate
C	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
C	0003941	molecular_function	L-serine ammonia-lyase activity
C	0004794	molecular_function	threonine deaminase activity
C	0006520	biological_process	amino acid metabolic process
C	0006565	biological_process	L-serine catabolic process
C	0006567	biological_process	L-threonine catabolic process
C	0016829	molecular_function	lyase activity
C	0016841	molecular_function	ammonia-lyase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0070689	biological_process	L-threonine catabolic process to propionate
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0003941	molecular_function	L-serine ammonia-lyase activity
D	0004794	molecular_function	threonine deaminase activity
D	0006520	biological_process	amino acid metabolic process
D	0006565	biological_process	L-serine catabolic process
D	0006567	biological_process	L-threonine catabolic process
D	0016829	molecular_function	lyase activity
D	0016841	molecular_function	ammonia-lyase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0070689	biological_process	L-threonine catabolic process to propionate

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 800

Chain	Residue
A	TYR220
A	ASP256
A	HOH801
A	HOH802
A	HOH803
D	ARG229

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA C 801

Chain	Residue
C	ASP256
C	HOH815
C	HOH983
B	ARG229
B	HOH338
C	TYR220

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLU49-ALA62

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1tdj

Chain	Residue	Details
A	SER311

---

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1tdj

Chain	Residue	Details
B	SER311

---

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1tdj

Chain	Residue	Details
C	SER311

---

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1tdj

Chain	Residue	Details
D	SER311

---