1J0D
ACC deaminase mutant complexed with ACC
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 | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 5PA A 1401 |
| Chain | Residue |
| A | LYS54 |
| A | SER166 |
| A | CYS200 |
| A | VAL201 |
| A | THR202 |
| A | GLY203 |
| A | SER204 |
| A | THR205 |
| A | TYR295 |
| A | GLU296 |
| A | HOH1467 |
| A | GLY74 |
| A | HOH1477 |
| A | GLY75 |
| A | SER78 |
| A | ASN79 |
| A | GLN80 |
| A | TRP102 |
| A | ALA163 |
| A | GLY164 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE 5PA B 1501 |
| Chain | Residue |
| B | ASN50 |
| B | LYS54 |
| B | SER78 |
| B | ASN79 |
| B | GLN80 |
| B | GLY164 |
| B | CYS200 |
| B | VAL201 |
| B | THR202 |
| B | GLY203 |
| B | SER204 |
| B | THR205 |
| B | TYR295 |
| B | GLU296 |
| B | LEU323 |
| B | GLY324 |
| B | GLY325 |
| B | HOH1507 |
| B | HOH1574 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 5PA C 1601 |
| Chain | Residue |
| C | ASN50 |
| C | LYS54 |
| C | SER78 |
| C | ASN79 |
| C | GLN80 |
| C | GLY164 |
| C | CYS200 |
| C | VAL201 |
| C | THR202 |
| C | GLY203 |
| C | THR205 |
| C | TYR295 |
| C | GLU296 |
| C | LEU323 |
| C | GLY324 |
| C | GLY325 |
| C | HOH1603 |
| C | HOH1611 |
| C | HOH1734 |
| C | HOH1736 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 5PA D 1701 |
| Chain | Residue |
| D | ASN50 |
| D | LYS54 |
| D | SER78 |
| D | ASN79 |
| D | GLN80 |
| D | ALA163 |
| D | GLY164 |
| D | VAL201 |
| D | THR202 |
| D | GLY203 |
| D | SER204 |
| D | THR205 |
| D | TYR295 |
| D | GLU296 |
| D | LEU323 |
| D | GLY324 |
| D | GLY325 |
| D | HOH1710 |
| D | HOH1760 |
| D | HOH1820 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"9604000","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
| Chain | Residue | Details |
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 | THR51 | |
| A | GLU296 | |
| A | SER78 | |
| A | TYR295 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| B | THR51 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| C | THR51 |
| site_id | CSA12 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| D | THR51 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| B | THR81 | |
| B | THR51 | |
| B | GLU296 | |
| B | SER78 | |
| B | TYR295 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| C | THR81 | |
| C | THR51 | |
| C | GLU296 | |
| C | SER78 | |
| C | TYR295 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| D | THR81 | |
| D | THR51 | |
| D | GLU296 | |
| D | SER78 | |
| D | TYR295 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| A | GLY48 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| B | GLY48 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| C | GLY48 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| D | GLY48 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1f2d |
| Chain | Residue | Details |
| A | THR51 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 545 |
| Chain | Residue | Details |
| A | THR51 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | TYR269 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
| A | TYR295 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 545 |
| Chain | Residue | Details |
| B | THR51 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | TYR269 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
| B | TYR295 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 545 |
| Chain | Residue | Details |
| C | THR51 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | TYR269 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
| C | TYR295 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 545 |
| Chain | Residue | Details |
| D | THR51 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | TYR269 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
| D | TYR295 | electrostatic stabiliser, proton acceptor, proton donor |
