2HOR

Crystal structure of alliinase from garlic- apo form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005773	cellular_component	vacuole
A	0006520	biological_process	amino acid metabolic process
A	0008483	molecular_function	transaminase activity
A	0016829	molecular_function	lyase activity
A	0016846	molecular_function	carbon-sulfur lyase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0031404	molecular_function	chloride ion binding
A	0042803	molecular_function	protein homodimerization activity
A	0047654	molecular_function	alliin lyase activity

Functional Information from PROSITE/UniProt

site_id	PS00022
Number of Residues	12
Details	EGF_1 EGF-like domain signature 1. CeCntCytGPdC

Chain	Residue	Details
A	CYS39-CYS50

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:12235163, ECO:0007744|PDB:1LK9

Chain	Residue	Details
A	TYR92

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:12235163, ECO:0007744|PDB:1LK9

Chain	Residue	Details
A	LYS251

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498

Chain	Residue	Details
A	ASN19

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:12235163, ECO:0000269|PubMed:17174334, ECO:0007744|PDB:1LK9, ECO:0007744|PDB:2HOX

Chain	Residue	Details
A	ASN328
A	ASN146

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site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:17174334, ECO:0007744|PDB:2HOX

Chain	Residue	Details
A	ASN191

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