3L6R
The structure of mammalian serine racemase: Evidence for conformational changes upon inhibitor binding
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0009069 | biological_process | serine family amino acid metabolic process |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0014070 | biological_process | response to organic cyclic compound |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MLI A 347 |
| Chain | Residue |
| A | LLP56 |
| A | HOH585 |
| A | HOH658 |
| A | SER83 |
| A | SER84 |
| A | ASN86 |
| A | HIS87 |
| A | ARG135 |
| A | GLY239 |
| A | SER242 |
| A | HOH461 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 348 |
| Chain | Residue |
| A | GLU210 |
| A | ALA214 |
| A | ASP216 |
| A | HOH411 |
| A | HOH696 |
| A | HOH702 |
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 | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:O59791 |
| Chain | Residue | Details |
| A | LLP56 | |
| A | SER84 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:35410329, ECO:0007744|PDB:7NBH |
| Chain | Residue | Details |
| A | GLU13 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:35410329, ECO:0007744|PDB:6ZSP |
| Chain | Residue | Details |
| A | SER31 | |
| A | SER32 | |
| A | ILE33 | |
| A | LYS51 | |
| A | THR52 | |
| A | GLN89 | |
| A | TYR121 | |
| A | LYS279 | |
| A | ASN316 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:35410329, ECO:0007744|PDB:7NBC, ECO:0007744|PDB:7NBF |
| Chain | Residue | Details |
| A | PRO69 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:35410329, ECO:0007744|PDB:7NBD |
| Chain | Residue | Details |
| A | THR81 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20106978, ECO:0000269|PubMed:29277459, ECO:0000269|PubMed:35410329, ECO:0007744|PDB:3L6B, ECO:0007744|PDB:5X2L, ECO:0007744|PDB:7NBC, ECO:0007744|PDB:7NBD, ECO:0007744|PDB:7NBF, ECO:0007744|PDB:7NBG |
| Chain | Residue | Details |
| A | ASN86 | |
| A | GLY185 | |
| A | GLY186 | |
| A | GLY187 | |
| A | GLY188 | |
| A | MSE189 | |
| A | SER313 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q76EQ0 |
| Chain | Residue | Details |
| A | ASN154 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:32039887, ECO:0000269|PubMed:35410329, ECO:0007744|PDB:6SLH, ECO:0007744|PDB:6ZUJ, ECO:0007744|PDB:7NBD |
| Chain | Residue | Details |
| A | ASP178 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20106978, ECO:0000269|PubMed:35410329, ECO:0007744|PDB:3L6B, ECO:0007744|PDB:3L6R |
| Chain | Residue | Details |
| A | GLU210 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20106978, ECO:0007744|PDB:3L6B, ECO:0007744|PDB:3L6R |
| Chain | Residue | Details |
| A | ALA214 | |
| A | ASP216 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:35410329, ECO:0007744|PDB:7NBC, ECO:0007744|PDB:7NBD, ECO:0007744|PDB:7NBF, ECO:0007744|PDB:7NBG, ECO:0007744|PDB:7NBH |
| Chain | Residue | Details |
| A | ASN247 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:20106978, ECO:0000269|PubMed:29277459, ECO:0000269|PubMed:35410329, ECO:0007744|PDB:3L6B, ECO:0007744|PDB:5X2L, ECO:0007744|PDB:7NBC, ECO:0007744|PDB:7NBD, ECO:0007744|PDB:7NBF, ECO:0007744|PDB:7NBG |
| Chain | Residue | Details |
| A | LLP56 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q9QZX7 |
| Chain | Residue | Details |
| A | CYS113 |
