7DLY
Crystal structure of Arabidopsis ACS7 mutant in complex with PPG
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009693 | biological_process | ethylene biosynthetic process |
| A | 0009835 | biological_process | fruit ripening |
| 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 |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009693 | biological_process | ethylene biosynthetic process |
| B | 0009835 | biological_process | fruit ripening |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016847 | molecular_function | 1-aminocyclopropane-1-carboxylate synthase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042218 | biological_process | 1-aminocyclopropane-1-carboxylate biosynthetic process |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue PPG A 1001 |
| Chain | Residue |
| A | TYR33 |
| A | ASN217 |
| A | ASP245 |
| A | ILE247 |
| A | TYR248 |
| A | SER282 |
| A | SER284 |
| A | LYS285 |
| A | ARG293 |
| A | ARG419 |
| A | LEU59 |
| A | ALA60 |
| A | GLU61 |
| A | GLY134 |
| A | ALA135 |
| A | THR136 |
| A | TYR160 |
| A | THR213 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue PPG B 1001 |
| Chain | Residue |
| B | TYR33 |
| B | ALA60 |
| B | GLU61 |
| B | ALA135 |
| B | THR136 |
| B | TYR160 |
| B | THR213 |
| B | ASN217 |
| B | ASP245 |
| B | ILE247 |
| B | TYR248 |
| B | SER282 |
| B | SER284 |
| B | LYS285 |
| B | ARG293 |
| B | ARG419 |
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 | SER282-GLY295 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU61 | |
| A | PHE100 | |
| B | GLU61 | |
| B | PHE100 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS285 | |
| B | LYS285 |
