Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008721 | molecular_function | D-serine ammonia-lyase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0036088 | biological_process | D-serine catabolic process |
| A | 0046416 | biological_process | D-amino acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 449 |
| Chain | Residue |
| A | ASN238 |
| A | SER239 |
| A | ARG240 |
| A | THR241 |
| A | HOH485 |
| A | HOH777 |
| A | HOH789 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 450 |
| Chain | Residue |
| A | GLY413 |
| A | HOH458 |
| A | HOH760 |
| A | HOH787 |
| A | ASN98 |
| A | GLY99 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 451 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 452 |
| Chain | Residue |
| A | ALA390 |
| A | ARG394 |
| A | HOH482 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 453 |
| Chain | Residue |
| A | ASN27 |
| A | GLY29 |
| A | GLU352 |
| A | ARG353 |
| A | HOH578 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA A 454 |
| Chain | Residue |
| A | CYS276 |
| A | GLY277 |
| A | GLU303 |
| A | SER307 |
| A | CYS309 |
| A | LEU338 |
| A | VAL340 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 455 |
| Chain | Residue |
| A | LYS116 |
| A | GLY277 |
| A | VAL278 |
| A | GLY279 |
| A | GLY280 |
| A | GLY281 |
| A | PRO282 |
| A | HOH831 |
| A | HOH835 |
| A | HOH841 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 456 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 457 |
| Chain | Residue |
| A | LYS116 |
| A | SER165 |
| A | THR166 |
| A | GLY167 |
| A | ASN168 |
| A | LEU169 |
| A | ASP236 |
| A | HOH834 |
| A | HOH841 |
Functional Information from PROSITE/UniProt
| site_id | PS00165 |
| Number of Residues | 15 |
| Details | DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. DshlaiSGSIKARGG |
| Chain | Residue | Details |
| A | ASP106-GLY120 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01030","evidenceCode":"ECO:0000255"}]} |
