1P5J

Crystal Structure Analysis of Human Serine Dehydratase

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	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
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	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	0042803	molecular_function	protein homodimerization activity
A	0042866	biological_process	pyruvate biosynthetic process
A	0044283	biological_process	small molecule biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP A 941

Chain	Residue
A	PHE40
A	LEU172
A	ALA269
A	CYS303
A	GLY304
A	GLY305
A	HOH418
A	HOH420
A	LYS41
A	ASN67
A	SER166
A	VAL167
A	GLY168
A	GLY169
A	GLY170
A	GLY171

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP32-ILE45

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16580895","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"15689518","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

---