1LK9
The Three-dimensional Structure of Alliinase from Garlic
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 |
B | 0005773 | cellular_component | vacuole |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0008483 | molecular_function | transaminase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0016846 | molecular_function | carbon-sulfur lyase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0031404 | molecular_function | chloride ion binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 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 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12235163, ECO:0007744|PDB:1LK9 |
Chain | Residue | Details |
A | TYR92 | |
B | TYR92 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:12235163, ECO:0007744|PDB:1LK9 |
Chain | Residue | Details |
A | LYS251 | |
B | LYS251 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
Chain | Residue | Details |
A | ASN19 | |
B | ASN19 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
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 | ASN146 | |
A | ASN328 | |
B | ASN146 | |
B | ASN328 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:17174334, ECO:0007744|PDB:2HOX |
Chain | Residue | Details |
A | ASN191 | |
B | ASN191 |