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1LK9

The Three-dimensional Structure of Alliinase from Garlic

Functional Information from GO Data
ChainGOidnamespacecontents
A0005773cellular_componentvacuole
A0006520biological_processamino acid metabolic process
A0008483molecular_functiontransaminase activity
A0016829molecular_functionlyase activity
A0016846molecular_functioncarbon-sulfur lyase activity
A0030170molecular_functionpyridoxal phosphate binding
A0031404molecular_functionchloride ion binding
A0042803molecular_functionprotein homodimerization activity
A0047654molecular_functionalliin lyase activity
B0005773cellular_componentvacuole
B0006520biological_processamino acid metabolic process
B0008483molecular_functiontransaminase activity
B0016829molecular_functionlyase activity
B0016846molecular_functioncarbon-sulfur lyase activity
B0030170molecular_functionpyridoxal phosphate binding
B0031404molecular_functionchloride ion binding
B0042803molecular_functionprotein homodimerization activity
B0047654molecular_functionalliin lyase activity
Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CeCntCytGPdC
ChainResidueDetails
ACYS39-CYS50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12235163, ECO:0007744|PDB:1LK9
ChainResidueDetails
ATYR92
BTYR92

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:12235163, ECO:0007744|PDB:1LK9
ChainResidueDetails
ALYS251
BLYS251

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN19
BASN19

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: 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
ChainResidueDetails
AASN146
AASN328
BASN146
BASN328

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:17174334, ECO:0007744|PDB:2HOX
ChainResidueDetails
AASN191
BASN191

218853

PDB entries from 2024-04-24

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