1TZM
Crystal structure of ACC deaminase complexed with substrate analog b-chloro-D-alanine
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 | 0018871 | biological_process | 1-aminocyclopropane-1-carboxylate metabolic process |
| 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 | 0018871 | biological_process | 1-aminocyclopropane-1-carboxylate metabolic process |
| 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 | 0018871 | biological_process | 1-aminocyclopropane-1-carboxylate metabolic process |
| 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 | 0018871 | biological_process | 1-aminocyclopropane-1-carboxylate metabolic process |
| 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 | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 701 |
| Chain | Residue |
| B | LYS51 |
| B | SER78 |
| B | ASN79 |
| B | GLN80 |
| B | TYR268 |
| B | TYR294 |
| B | PLP401 |
| B | HOH1037 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 D 702 |
| Chain | Residue |
| D | SER78 |
| D | ASN79 |
| D | GLN80 |
| D | TYR268 |
| D | TYR294 |
| D | PLP401 |
| D | HOH863 |
| D | HOH911 |
| D | LYS51 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE PLP A 401 |
| Chain | Residue |
| A | ASN50 |
| A | LYS51 |
| A | LYS54 |
| A | ASN79 |
| A | SER163 |
| A | CYS196 |
| A | SER197 |
| A | VAL198 |
| A | THR199 |
| A | GLY200 |
| A | SER201 |
| A | THR202 |
| A | TYR294 |
| A | GLU295 |
| A | LEU322 |
| A | GLY323 |
| A | GLY324 |
| A | C2N501 |
| A | NAK601 |
| A | HOH875 |
| A | HOH947 |
| A | HOH1034 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE C2N A 501 |
| Chain | Residue |
| A | LYS51 |
| A | ILE73 |
| A | GLY74 |
| A | SER78 |
| A | ASN79 |
| A | GLN80 |
| A | TRP102 |
| A | ALA160 |
| A | GLY161 |
| A | TYR268 |
| A | TYR294 |
| A | PLP401 |
| A | NAK601 |
| A | HOH801 |
| A | HOH876 |
| A | HOH1197 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE NAK A 601 |
| Chain | Residue |
| A | LYS51 |
| A | SER78 |
| A | ASN79 |
| A | GLN80 |
| A | THR199 |
| A | TYR294 |
| A | PLP401 |
| A | C2N501 |
| A | HOH801 |
| A | HOH1197 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP B 401 |
| Chain | Residue |
| B | ASN50 |
| B | LYS51 |
| B | LYS54 |
| B | ASN79 |
| B | SER197 |
| B | VAL198 |
| B | THR199 |
| B | GLY200 |
| B | THR202 |
| B | TYR294 |
| B | GLU295 |
| B | LEU322 |
| B | GLY323 |
| B | GLY324 |
| B | SO4701 |
| B | HOH877 |
| B | HOH929 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE PLP C 401 |
| Chain | Residue |
| C | NAK602 |
| C | HOH804 |
| C | HOH811 |
| C | ASN50 |
| C | LYS51 |
| C | LYS54 |
| C | ASN79 |
| C | SER163 |
| C | SER197 |
| C | VAL198 |
| C | THR199 |
| C | GLY200 |
| C | SER201 |
| C | THR202 |
| C | TYR294 |
| C | GLU295 |
| C | LEU322 |
| C | GLY323 |
| C | GLY324 |
| C | C2N502 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE C2N C 502 |
| Chain | Residue |
| C | GLY75 |
| C | SER78 |
| C | ASN79 |
| C | GLN80 |
| C | TYR268 |
| C | TYR294 |
| C | PLP401 |
| C | NAK602 |
| C | HOH802 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE NAK C 602 |
| Chain | Residue |
| C | LYS51 |
| C | SER78 |
| C | ASN79 |
| C | GLN80 |
| C | THR199 |
| C | TYR294 |
| C | PLP401 |
| C | C2N502 |
| C | HOH802 |
| C | HOH907 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP D 401 |
| Chain | Residue |
| D | ASN50 |
| D | LYS51 |
| D | LYS54 |
| D | ASN79 |
| D | CYS196 |
| D | SER197 |
| D | VAL198 |
| D | THR199 |
| D | GLY200 |
| D | THR202 |
| D | TYR294 |
| D | GLU295 |
| D | LEU322 |
| D | GLY323 |
| D | GLY324 |
| D | SO4702 |
| D | HOH810 |
| D | HOH884 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00807 |
| Chain | Residue | Details |
| A | SER78 | |
| B | SER78 | |
| C | SER78 | |
| D | SER78 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | LYS51 | |
| B | LYS51 | |
| C | LYS51 | |
| D | LYS51 |
