Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1PWE

Rat Liver L-Serine Dehydratase Apo Enzyme

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003941	molecular_function	L-serine ammonia-lyase activity
A	0004794	molecular_function	threonine deaminase activity
A	0005737	cellular_component	cytoplasm
A	0006094	biological_process	gluconeogenesis
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	0006629	biological_process	lipid metabolic process
A	0016829	molecular_function	lyase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0031667	biological_process	response to nutrient levels
A	0033590	biological_process	response to cobalamin
A	0042803	molecular_function	protein homodimerization activity
A	0042866	biological_process	pyruvate biosynthetic process
A	0043200	biological_process	response to amino acid
A	0044283	biological_process	small molecule biosynthetic process
A	0065003	biological_process	protein-containing complex assembly
B	0003941	molecular_function	L-serine ammonia-lyase activity
B	0004794	molecular_function	threonine deaminase activity
B	0005737	cellular_component	cytoplasm
B	0006094	biological_process	gluconeogenesis
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	0006629	biological_process	lipid metabolic process
B	0016829	molecular_function	lyase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0031667	biological_process	response to nutrient levels
B	0033590	biological_process	response to cobalamin
B	0042803	molecular_function	protein homodimerization activity
B	0042866	biological_process	pyruvate biosynthetic process
B	0043200	biological_process	response to amino acid
B	0044283	biological_process	small molecule biosynthetic process
B	0065003	biological_process	protein-containing complex assembly
C	0003941	molecular_function	L-serine ammonia-lyase activity
C	0004794	molecular_function	threonine deaminase activity
C	0005737	cellular_component	cytoplasm
C	0006094	biological_process	gluconeogenesis
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	0006629	biological_process	lipid metabolic process
C	0016829	molecular_function	lyase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0031667	biological_process	response to nutrient levels
C	0033590	biological_process	response to cobalamin
C	0042803	molecular_function	protein homodimerization activity
C	0042866	biological_process	pyruvate biosynthetic process
C	0043200	biological_process	response to amino acid
C	0044283	biological_process	small molecule biosynthetic process
C	0065003	biological_process	protein-containing complex assembly
D	0003941	molecular_function	L-serine ammonia-lyase activity
D	0004794	molecular_function	threonine deaminase activity
D	0005737	cellular_component	cytoplasm
D	0006094	biological_process	gluconeogenesis
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	0006629	biological_process	lipid metabolic process
D	0016829	molecular_function	lyase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0031667	biological_process	response to nutrient levels
D	0033590	biological_process	response to cobalamin
D	0042803	molecular_function	protein homodimerization activity
D	0042866	biological_process	pyruvate biosynthetic process
D	0043200	biological_process	response to amino acid
D	0044283	biological_process	small molecule biosynthetic process
D	0065003	biological_process	protein-containing complex assembly
E	0003941	molecular_function	L-serine ammonia-lyase activity
E	0004794	molecular_function	threonine deaminase activity
E	0005737	cellular_component	cytoplasm
E	0006094	biological_process	gluconeogenesis
E	0006520	biological_process	amino acid metabolic process
E	0006565	biological_process	L-serine catabolic process
E	0006567	biological_process	L-threonine catabolic process
E	0006629	biological_process	lipid metabolic process
E	0016829	molecular_function	lyase activity
E	0030170	molecular_function	pyridoxal phosphate binding
E	0031667	biological_process	response to nutrient levels
E	0033590	biological_process	response to cobalamin
E	0042803	molecular_function	protein homodimerization activity
E	0042866	biological_process	pyruvate biosynthetic process
E	0043200	biological_process	response to amino acid
E	0044283	biological_process	small molecule biosynthetic process
E	0065003	biological_process	protein-containing complex assembly
F	0003941	molecular_function	L-serine ammonia-lyase activity
F	0004794	molecular_function	threonine deaminase activity
F	0005737	cellular_component	cytoplasm
F	0006094	biological_process	gluconeogenesis
F	0006520	biological_process	amino acid metabolic process
F	0006565	biological_process	L-serine catabolic process
F	0006567	biological_process	L-threonine catabolic process
F	0006629	biological_process	lipid metabolic process
F	0016829	molecular_function	lyase activity
F	0030170	molecular_function	pyridoxal phosphate binding
F	0031667	biological_process	response to nutrient levels
F	0033590	biological_process	response to cobalamin
F	0042803	molecular_function	protein homodimerization activity
F	0042866	biological_process	pyruvate biosynthetic process
F	0043200	biological_process	response to amino acid
F	0044283	biological_process	small molecule biosynthetic process
F	0065003	biological_process	protein-containing complex assembly

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP32-ILE45

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P20132","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"14596599","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2228555","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2660911","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	LYS41

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

Chain	Residue	Details
B	LYS41

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

Chain	Residue	Details
C	LYS41

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

Chain	Residue	Details
D	LYS41

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1pwh

Chain	Residue	Details
E	LYS41

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1pwh

Chain	Residue	Details
F	LYS41

site_id	MCSA1
Number of Residues	3
Details	M-CSA 186

Chain	Residue	Details
A	LYS41	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
A	ALA222	electrostatic stabiliser, hydrogen bond acceptor
A	CYS303	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	3
Details	M-CSA 186

Chain	Residue	Details
B	LYS41	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
B	ALA222	electrostatic stabiliser, hydrogen bond acceptor
B	CYS303	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	3
Details	M-CSA 186

Chain	Residue	Details
C	LYS41	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
C	ALA222	electrostatic stabiliser, hydrogen bond acceptor
C	CYS303	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	3
Details	M-CSA 186

Chain	Residue	Details
D	LYS41	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
D	ALA222	electrostatic stabiliser, hydrogen bond acceptor
D	CYS303	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA5
Number of Residues	3
Details	M-CSA 186

Chain	Residue	Details
E	LYS41	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
E	ALA222	electrostatic stabiliser, hydrogen bond acceptor
E	CYS303	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA6
Number of Residues	3
Details	M-CSA 186

Chain	Residue	Details
F	LYS41	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
F	ALA222	electrostatic stabiliser, hydrogen bond acceptor
F	CYS303	electrostatic stabiliser, hydrogen bond donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)