Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1PWH

Rat Liver L-Serine Dehydratase- Complex with PYRIDOXYL-(O-METHYL-SERINE)-5-MONOPHOSPHATE

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	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006520	biological_process	amino acid metabolic process
A	0006565	biological_process	L-serine 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	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0006094	biological_process	gluconeogenesis
B	0006520	biological_process	amino acid metabolic process
B	0006565	biological_process	L-serine 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	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0006094	biological_process	gluconeogenesis
C	0006520	biological_process	amino acid metabolic process
C	0006565	biological_process	L-serine 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	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0006094	biological_process	gluconeogenesis
D	0006520	biological_process	amino acid metabolic process
D	0006565	biological_process	L-serine 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K A 332

Chain	Residue
A	VAL167
A	GLY168
A	GLU194
A	ALA198
A	SER200
A	LEU223

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K B 333

Chain	Residue
B	ALA198
B	SER200
B	LEU223
B	VAL167
B	GLY168
B	GLU194

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 334

Chain	Residue
C	VAL167
C	GLY168
C	GLU194
C	ALA198
C	SER200
C	LEU223

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K D 335

Chain	Residue
D	VAL167
D	GLY168
D	GLU194
D	ALA198
D	SER200
D	LEU223

site_id	AC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE PLV A 328

Chain	Residue
A	PHE40
A	LYS41
A	SER64
A	ALA65
A	ASN67
A	ALA68
A	PRO135
A	PHE136
A	SER166
A	VAL167
A	GLY168
A	GLY169
A	GLY170
A	GLY171
A	LEU172
A	LYS221
A	ALA222
A	GLY224
A	CYS303
A	GLY304
A	HOH334
A	HOH350
A	HOH356

site_id	AC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE PLV B 329

Chain	Residue
B	PHE40
B	LYS41
B	SER64
B	ALA65
B	ASN67
B	ALA68
B	PHE136
B	SER166
B	GLY168
B	GLY169
B	GLY170
B	GLY171
B	LEU172
B	LYS221
B	ALA222
B	GLY224
B	CYS303
B	HOH334
B	HOH336
B	HOH347

site_id	AC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE PLV C 330

Chain	Residue
C	PHE40
C	LYS41
C	SER64
C	ALA65
C	ASN67
C	ALA68
C	PRO135
C	PHE136
C	SER166
C	VAL167
C	GLY168
C	GLY169
C	GLY170
C	GLY171
C	LEU172
C	LYS221
C	ALA222
C	GLY224
C	CYS303
C	HOH337
C	HOH339

site_id	AC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE PLV D 331

Chain	Residue
D	GLY170
D	GLY171
D	LEU172
D	LYS221
D	ALA222
D	GLY224
D	CYS303
D	HOH336
D	HOH339
D	PHE40
D	LYS41
D	SER64
D	ALA65
D	ASN67
D	ALA68
D	PHE136
D	SER166
D	VAL167
D	GLY168
D	GLY169

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	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P20132","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"2660911","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
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	a catalytic site defined by CSA, PubMed 14596599

Chain	Residue	Details
A	LYS41

site_id	CSA2
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 14596599

Chain	Residue	Details
B	LYS41

site_id	CSA3
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 14596599

Chain	Residue	Details
C	LYS41

site_id	CSA4
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 14596599

Chain	Residue	Details
D	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

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