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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 46 |
| Details | Domain: {"description":"EGF-like; atypical"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12235163","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LK9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"12235163","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LK9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12235163","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17174334","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LK9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HOX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17174334","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HOX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP225 | |
| A | TYR165 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | PRO96 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS251 | |
| A | ASP225 | |
| A | TYR165 |
