3L6C
X-ray crystal structure of rat serine racemase in complex with malonate a potent inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006563 | biological_process | L-serine metabolic process |
| A | 0008721 | molecular_function | D-serine ammonia-lyase activity |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0016594 | molecular_function | glycine binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0018114 | molecular_function | threonine racemase activity |
| A | 0030165 | molecular_function | PDZ domain binding |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0030378 | molecular_function | serine racemase activity |
| A | 0032496 | biological_process | response to lipopolysaccharide |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042866 | biological_process | pyruvate biosynthetic process |
| A | 0043025 | cellular_component | neuronal cell body |
| A | 0045177 | cellular_component | apical part of cell |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070178 | biological_process | D-serine metabolic process |
| A | 0070179 | biological_process | D-serine biosynthetic process |
| A | 1901986 | biological_process | response to ketamine |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006563 | biological_process | L-serine metabolic process |
| B | 0008721 | molecular_function | D-serine ammonia-lyase activity |
| B | 0009410 | biological_process | response to xenobiotic stimulus |
| B | 0016594 | molecular_function | glycine binding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0018114 | molecular_function | threonine racemase activity |
| B | 0030165 | molecular_function | PDZ domain binding |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0030378 | molecular_function | serine racemase activity |
| B | 0032496 | biological_process | response to lipopolysaccharide |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042866 | biological_process | pyruvate biosynthetic process |
| B | 0043025 | cellular_component | neuronal cell body |
| B | 0045177 | cellular_component | apical part of cell |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070178 | biological_process | D-serine metabolic process |
| B | 0070179 | biological_process | D-serine biosynthetic process |
| B | 1901986 | biological_process | response to ketamine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP A 350 |
| Chain | Residue |
| A | PHE55 |
| A | GLY239 |
| A | VAL240 |
| A | THR285 |
| A | SER313 |
| A | MLI341 |
| A | HOH346 |
| A | HOH355 |
| A | HOH358 |
| A | LYS56 |
| A | ASN86 |
| A | ASN154 |
| A | GLY185 |
| A | GLY186 |
| A | GLY187 |
| A | GLY188 |
| A | MET189 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 340 |
| Chain | Residue |
| A | GLU210 |
| A | ALA214 |
| A | ASP216 |
| A | HOH388 |
| A | HOH389 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MLI A 341 |
| Chain | Residue |
| A | LYS56 |
| A | SER83 |
| A | SER84 |
| A | ASN86 |
| A | HIS87 |
| A | ARG135 |
| A | SER242 |
| A | PLP350 |
| A | HOH355 |
| A | HOH365 |
| A | HOH393 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 350 |
| Chain | Residue |
| B | PHE55 |
| B | LYS56 |
| B | ASN86 |
| B | PRO183 |
| B | VAL184 |
| B | GLY185 |
| B | GLY186 |
| B | GLY187 |
| B | GLY188 |
| B | MET189 |
| B | GLU283 |
| B | THR285 |
| B | SER313 |
| B | HOH345 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN B 340 |
| Chain | Residue |
| B | GLU210 |
| B | ALA214 |
| B | ASP216 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MLI B 341 |
| Chain | Residue |
| B | LYS56 |
| B | SER83 |
| B | SER84 |
| B | GLY85 |
| B | ASN86 |
| B | HIS87 |
| B | ARG135 |
| B | GLY239 |
| B | SER242 |
Functional Information from PROSITE/UniProt
| site_id | PS00165 |
| Number of Residues | 14 |
| Details | DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Elfqk.TGSFKIRGA |
| Chain | Residue | Details |
| A | GLU47-ALA60 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"O59791","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 27 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9GZT4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20106978","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HMK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L6C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20106978","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3L6C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"20106978","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HMK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L6C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9QZX7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"Q9QZX7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
