6QKB
Crystal structure of the beta-hydroxyaspartate aldolase of Paracoccus denitrificans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0008721 | molecular_function | D-serine ammonia-lyase activity |
| A | 0009436 | biological_process | glyoxylate catabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016833 | molecular_function | oxo-acid-lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0036088 | biological_process | D-serine catabolic process |
| A | 0046296 | biological_process | glycolate catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0008721 | molecular_function | D-serine ammonia-lyase activity |
| B | 0009436 | biological_process | glyoxylate catabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016833 | molecular_function | oxo-acid-lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0036088 | biological_process | D-serine catabolic process |
| B | 0046296 | biological_process | glycolate catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue PLP A 401 |
| Chain | Residue |
| A | HIS60 |
| A | GLN254 |
| A | GLY256 |
| A | SER257 |
| A | TYR265 |
| A | HOH568 |
| A | HOH569 |
| A | HOH608 |
| A | LYS62 |
| A | GLN85 |
| A | THR104 |
| A | ARG162 |
| A | GLN190 |
| A | TYR192 |
| A | GLY237 |
| A | THR238 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | HIS355 |
| A | ASP357 |
| A | HOH513 |
| A | HOH608 |
| A | HOH792 |
| B | HOH502 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| A | HOH507 |
| B | HIS355 |
| B | ASP357 |
| B | HOH508 |
| B | HOH719 |
| B | HOH836 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | binding site for Di-peptide PLP B 401 and LYS B 62 |
| Chain | Residue |
| A | LYS307 |
| A | HOH503 |
| B | HIS60 |
| B | GLY61 |
| B | MET63 |
| B | HIS64 |
| B | CYS83 |
| B | GLN85 |
| B | GLN190 |
| B | TYR192 |
| B | GLY237 |
| B | THR238 |
| B | GLN254 |
| B | GLY256 |
| B | SER257 |
| B | TYR265 |
| B | HOH503 |
| B | HOH562 |
| B | HOH622 |
| B | HOH663 |
| B | HOH719 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31723261","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"31723261","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
