Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2RKB

Serine dehydratase like-1 from human cancer cells

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	0005829	cellular_component	cytosol
A	0006520	biological_process	amino acid metabolic process
A	0006565	biological_process	L-serine catabolic process
A	0006567	biological_process	threonine catabolic process
A	0006629	biological_process	lipid metabolic process
A	0008881	molecular_function	glutamate racemase activity
A	0009097	biological_process	isoleucine biosynthetic process
A	0016829	molecular_function	lyase activity
A	0016853	molecular_function	isomerase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
B	0003941	molecular_function	L-serine ammonia-lyase activity
B	0004794	molecular_function	threonine deaminase activity
B	0005829	cellular_component	cytosol
B	0006520	biological_process	amino acid metabolic process
B	0006565	biological_process	L-serine catabolic process
B	0006567	biological_process	threonine catabolic process
B	0006629	biological_process	lipid metabolic process
B	0008881	molecular_function	glutamate racemase activity
B	0009097	biological_process	isoleucine biosynthetic process
B	0016829	molecular_function	lyase activity
B	0016853	molecular_function	isomerase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042802	molecular_function	identical protein binding
C	0003941	molecular_function	L-serine ammonia-lyase activity
C	0004794	molecular_function	threonine deaminase activity
C	0005829	cellular_component	cytosol
C	0006520	biological_process	amino acid metabolic process
C	0006565	biological_process	L-serine catabolic process
C	0006567	biological_process	threonine catabolic process
C	0006629	biological_process	lipid metabolic process
C	0008881	molecular_function	glutamate racemase activity
C	0009097	biological_process	isoleucine biosynthetic process
C	0016829	molecular_function	lyase activity
C	0016853	molecular_function	isomerase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0042802	molecular_function	identical protein binding
D	0003941	molecular_function	L-serine ammonia-lyase activity
D	0004794	molecular_function	threonine deaminase activity
D	0005829	cellular_component	cytosol
D	0006520	biological_process	amino acid metabolic process
D	0006565	biological_process	L-serine catabolic process
D	0006567	biological_process	threonine catabolic process
D	0006629	biological_process	lipid metabolic process
D	0008881	molecular_function	glutamate racemase activity
D	0009097	biological_process	isoleucine biosynthetic process
D	0016829	molecular_function	lyase activity
D	0016853	molecular_function	isomerase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0042802	molecular_function	identical protein binding
E	0003941	molecular_function	L-serine ammonia-lyase activity
E	0004794	molecular_function	threonine deaminase activity
E	0005829	cellular_component	cytosol
E	0006520	biological_process	amino acid metabolic process
E	0006565	biological_process	L-serine catabolic process
E	0006567	biological_process	threonine catabolic process
E	0006629	biological_process	lipid metabolic process
E	0008881	molecular_function	glutamate racemase activity
E	0009097	biological_process	isoleucine biosynthetic process
E	0016829	molecular_function	lyase activity
E	0016853	molecular_function	isomerase activity
E	0030170	molecular_function	pyridoxal phosphate binding
E	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 401

Chain	Residue
A	GLY174
A	GLU200
A	ALA204
A	CYS206
A	LEU229

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K B 401

Chain	Residue
B	LEU229
B	GLY174
B	GLU200
B	ALA204
B	CYS206

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K C 401

Chain	Residue
C	GLY174
C	GLU200
C	ALA204
C	CYS206
C	LEU229

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K D 401

Chain	Residue
D	GLY174
D	GLU200
D	ALA204
D	CYS206
D	LEU229

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K E 401

Chain	Residue
E	GLY174
E	GLU200
E	ALA204
E	CYS206
E	LEU229

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP A 400

Chain	Residue
A	PHE47
A	LYS48
A	ASN74
A	PHE142
A	GLY174
A	GLY175
A	GLY176
A	GLY177
A	LEU178
A	SER228
A	CYS309
A	HOH405
A	HOH407

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP B 400

Chain	Residue
B	PHE47
B	LYS48
B	ASN74
B	PHE142
B	GLY174
B	GLY175
B	GLY176
B	GLY177
B	LEU178
B	SER228
B	CYS309
B	HOH405
B	HOH439
B	HOH463

site_id	AC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP C 400

Chain	Residue
C	PHE47
C	LYS48
C	ASN74
C	PHE142
C	GLY174
C	GLY175
C	GLY176
C	GLY177
C	LEU178
C	SER228
C	CYS309
C	HOH416
C	HOH427

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PLP D 400

Chain	Residue
D	PHE47
D	LYS48
D	ASN74
D	PHE142
D	GLY174
D	GLY175
D	GLY176
D	GLY177
D	LEU178
D	SER228
D	CYS309

site_id	BC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP E 400

Chain	Residue
E	PHE47
E	LYS48
E	ASN74
E	PHE142
E	GLY174
E	GLY175
E	GLY176
E	GLY177
E	LEU178
E	SER228
E	CYS309
E	HOH466
E	HOH482

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLU39-ILE52

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269\|PubMed:18342636

Chain	Residue	Details
A	LYS48
B	LYS48
C	LYS48
D	LYS48
E	LYS48

Catalytic Information from CSA

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

Chain	Residue	Details
A	LYS48

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

Chain	Residue	Details
B	LYS48

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

Chain	Residue	Details
C	LYS48

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

Chain	Residue	Details
D	LYS48

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

Chain	Residue	Details
E	LYS48

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)