1M4N
CRYSTAL STRUCTURE OF APPLE ACC SYNTHASE IN COMPLEX WITH [2-(AMINO-OXY)ETHYL](5'-DEOXYADENOSIN-5'-YL)(METHYL)SULFONIUM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009693 | biological_process | ethylene biosynthetic process |
| A | 0009835 | biological_process | fruit ripening |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016847 | molecular_function | 1-aminocyclopropane-1-carboxylate synthase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042218 | biological_process | 1-aminocyclopropane-1-carboxylate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 501 |
| Chain | Residue |
| A | GLY119 |
| A | SER270 |
| A | SER272 |
| A | LYS273 |
| A | ARG281 |
| A | AAD502 |
| A | HOH768 |
| A | ALA120 |
| A | THR121 |
| A | TYR145 |
| A | THR198 |
| A | ASN202 |
| A | ASP230 |
| A | ILE232 |
| A | TYR233 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE AAD A 502 |
| Chain | Residue |
| A | GLN83 |
| A | ASP84 |
| A | TYR85 |
| A | THR121 |
| A | TYR145 |
| A | GLY147 |
| A | ARG150 |
| A | ASP151 |
| A | LYS273 |
| A | SER301 |
| A | PLP501 |
| A | MES601 |
| A | HOH619 |
| A | HOH624 |
| A | HOH685 |
| A | HOH717 |
| A | HOH776 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES A 601 |
| Chain | Residue |
| A | GLY44 |
| A | LEU45 |
| A | ALA46 |
| A | GLU47 |
| A | TYR145 |
| A | LYS273 |
| A | ARG407 |
| A | AAD502 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SLSKdlGLpGFRVG |
| Chain | Residue | Details |
| A | SER270-GLY283 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12686108","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1M4N","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12686108","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1B8G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M4N","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":"10610793","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9398277","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B8G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PIU","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 | TYR145 | |
| A | ASP230 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ALA90 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS273 | |
| A | TYR145 | |
| A | ASP230 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 418 |
| Chain | Residue | Details |
| A | TYR145 | activator, steric role |
| A | ASP230 | electrostatic stabiliser |
| A | ILE232 | steric role |
| A | LYS273 | covalent catalysis, proton shuttle (general acid/base) |
