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: BINDING => ECO:0000269|PubMed:31723261 |
Chain | Residue | Details |
A | GLN85 | |
B | TYR265 | |
B | HIS355 | |
B | ASP357 | |
A | THR238 | |
A | GLY256 | |
A | TYR265 | |
A | HIS355 | |
A | ASP357 | |
B | GLN85 | |
B | THR238 | |
B | GLY256 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:31723261 |
Chain | Residue | Details |
A | LYS62 | |
B | LYS62 |