1J0E
ACC deaminase mutant reacton intermediate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008660 | molecular_function | 1-aminocyclopropane-1-carboxylate deaminase activity |
| A | 0009310 | biological_process | amine catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016846 | molecular_function | carbon-sulfur lyase activity |
| A | 0019148 | molecular_function | D-cysteine desulfhydrase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0008660 | molecular_function | 1-aminocyclopropane-1-carboxylate deaminase activity |
| B | 0009310 | biological_process | amine catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016846 | molecular_function | carbon-sulfur lyase activity |
| B | 0019148 | molecular_function | D-cysteine desulfhydrase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0008660 | molecular_function | 1-aminocyclopropane-1-carboxylate deaminase activity |
| C | 0009310 | biological_process | amine catabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016846 | molecular_function | carbon-sulfur lyase activity |
| C | 0019148 | molecular_function | D-cysteine desulfhydrase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0008660 | molecular_function | 1-aminocyclopropane-1-carboxylate deaminase activity |
| D | 0009310 | biological_process | amine catabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016846 | molecular_function | carbon-sulfur lyase activity |
| D | 0019148 | molecular_function | D-cysteine desulfhydrase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 1AC A 1001 |
| Chain | Residue |
| A | SER78 |
| A | ASN79 |
| A | GLN80 |
| A | PHE295 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1AC B 2001 |
| Chain | Residue |
| B | HOH2125 |
| B | SER78 |
| B | ASN79 |
| B | GLN80 |
| B | PHE295 |
| B | HOH2124 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 1AC C 3001 |
| Chain | Residue |
| C | SER78 |
| C | ASN79 |
| C | GLN80 |
| C | TRP102 |
| C | PHE295 |
| C | HOH3003 |
| C | HOH3011 |
| C | HOH3373 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 1AC D 4001 |
| Chain | Residue |
| D | SER78 |
| D | ASN79 |
| D | GLN80 |
| D | TRP102 |
| D | PHE295 |
| D | HOH4031 |
| D | HOH4061 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | SER78 | |
| B | SER78 | |
| C | SER78 | |
| D | SER78 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:9604000 |
| Chain | Residue | Details |
| A | ALA1 | |
| B | ALA1 | |
| C | ALA1 | |
| D | ALA1 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | LLP51 | |
| B | LLP51 | |
| C | LLP51 | |
| D | LLP51 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| A | THR81 | |
| A | LYS51 | |
| A | GLU296 | |
| A | SER78 | |
| A | PHE295 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| B | THR81 | |
| B | LYS51 | |
| B | GLU296 | |
| B | SER78 | |
| B | PHE295 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| C | THR81 | |
| C | LYS51 | |
| C | GLU296 | |
| C | SER78 | |
| C | PHE295 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| D | THR81 | |
| D | LYS51 | |
| D | GLU296 | |
| D | SER78 | |
| D | PHE295 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| A | LYS51 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| B | LYS51 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| C | LYS51 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| D | LYS51 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 545 |
| Chain | Residue | Details |
| A | LLP51 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | ASN273 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
| A | SER299 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 545 |
| Chain | Residue | Details |
| B | LLP51 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | ASN273 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
| B | SER299 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 545 |
| Chain | Residue | Details |
| C | LLP51 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | ASN273 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
| C | SER299 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 545 |
| Chain | Residue | Details |
| D | LLP51 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | ASN273 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
| D | SER299 | electrostatic stabiliser, proton acceptor, proton donor |
