2ISQ

Crystal Structure of O-Acetylserine Sulfhydrylase from Arabidopsis Thaliana in Complex with C-Terminal Peptide from Arabidopsis Serine Acetyltransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000325	cellular_component	plant-type vacuole
A	0003729	molecular_function	mRNA binding
A	0004124	molecular_function	cysteine synthase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005777	cellular_component	peroxisome
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006535	biological_process	cysteine biosynthetic process from serine
A	0008652	biological_process	amino acid biosynthetic process
A	0009507	cellular_component	chloroplast
A	0009567	biological_process	double fertilization forming a zygote and endosperm
A	0009570	cellular_component	chloroplast stroma
A	0009860	biological_process	pollen tube growth
A	0016740	molecular_function	transferase activity
A	0019344	biological_process	cysteine biosynthetic process
A	0046686	biological_process	response to cadmium ion
A	0048046	cellular_component	apoplast
A	1900056	biological_process	negative regulation of leaf senescence

Functional Information from PDB Data

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP A 400

Functional Information from PROSITE/UniProt

site_id	PS00901
Number of Residues	19
Details	CYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KlEmme.PCsSVKdRiGfsM

Chain	Residue	Details
A	LYS35-MET53

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	143
Details	Region: {"description":"SUTR1;2 binding","evidences":[{"source":"PubMed","id":"20529854","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	5
Details	Region: {"description":"SAT1 binding","evidences":[{"source":"PubMed","id":"16166087","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16166087","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17194764","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Z7W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ISQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"16166087","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17194764","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Z7W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ISQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22092075","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1oas

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

Chain	Residue	Details
A	LYS46

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1oas