3PCV
Crystal structure analysis of human leukotriene C4 synthase at 1.9 angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004364 | molecular_function | glutathione transferase activity |
| A | 0004464 | molecular_function | leukotriene-C4 synthase activity |
| A | 0004602 | molecular_function | glutathione peroxidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005635 | cellular_component | nuclear envelope |
| A | 0005640 | cellular_component | nuclear outer membrane |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006691 | biological_process | leukotriene metabolic process |
| A | 0008047 | molecular_function | enzyme activator activity |
| A | 0008289 | molecular_function | lipid binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019370 | biological_process | leukotriene biosynthetic process |
| A | 0031965 | cellular_component | nuclear membrane |
| A | 0042759 | biological_process | long-chain fatty acid biosynthetic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE GSH A 201 |
| Chain | Residue |
| A | SER23 |
| A | TYR93 |
| A | TYR97 |
| A | ARG104 |
| A | LEU108 |
| A | EDO217 |
| A | HOH303 |
| A | ILE27 |
| A | ARG30 |
| A | TYR50 |
| A | ARG51 |
| A | GLN53 |
| A | ASN55 |
| A | GLU58 |
| A | TYR59 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LMT A 203 |
| Chain | Residue |
| A | LEU7 |
| A | LEU127 |
| A | PHE130 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LMT A 204 |
| Chain | Residue |
| A | ALA20 |
| A | TRP116 |
| A | EDO217 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE LMT A 205 |
| Chain | Residue |
| A | LEU18 |
| A | GLN95 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LMT A 206 |
| Chain | Residue |
| A | PHE74 |
| A | ALA128 |
| A | PRO132 |
| A | LEU135 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LMT A 207 |
| Chain | Residue |
| A | ALA10 |
| A | GLY77 |
| A | LEU81 |
| A | LEU84 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE LMT A 208 |
| Chain | Residue |
| A | MET1 |
| A | ILE72 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE LMT A 209 |
| Chain | Residue |
| A | TRP116 |
| A | LEU117 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE LMT A 211 |
| Chain | Residue |
| A | LEU84 |
| A | PHE88 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE LMT A 213 |
| Chain | Residue |
| A | LEU18 |
| A | PHE88 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 214 |
| Chain | Residue |
| A | THR40 |
| A | TYR50 |
| A | TYR50 |
| A | ARG51 |
| A | HOH314 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 215 |
| Chain | Residue |
| A | GLN19 |
| A | SER23 |
| A | SER57 |
| A | GLU58 |
| A | LEU62 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 216 |
| Chain | Residue |
| A | SER36 |
| A | ARG104 |
| A | EDO217 |
| A | HOH333 |
| A | HOH381 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 217 |
| Chain | Residue |
| A | GSH201 |
| A | LMT204 |
| A | EDO216 |
| A | HOH382 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 250 |
| Chain | Residue |
| A | SER100 |
| A | SER100 |
| A | ALA101 |
| A | ALA101 |
| A | GLN102 |
| A | GLN102 |
| A | HOH307 |
| A | HOH307 |
| A | HOH336 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 251 |
| Chain | Residue |
| A | ARG34 |
| A | ARG34 |
| A | ARG34 |
| A | HOH398 |
| A | HOH398 |
| A | HOH398 |
Functional Information from PROSITE/UniProt
| site_id | PS01297 |
| Number of Residues | 15 |
| Details | FLAP_GST2_LTC4S FLAP/GST2/LTC4S family signature. GppeFERVYrAQvNC |
| Chain | Residue | Details |
| A | GLY42-CYS56 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 33 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:12023288, ECO:0000305|PubMed:17632546, ECO:0000305|PubMed:17632548 |
| Chain | Residue | Details |
| A | MET1-ALA6 | |
| A | ALA70-PHE73 | |
| A | GLY125-ALA150 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 79 |
| Details | TRANSMEM: Helical => ECO:0000305|PubMed:12023288, ECO:0000305|PubMed:17632546, ECO:0000305|PubMed:17632548 |
| Chain | Residue | Details |
| A | LEU7-ILE27 | |
| A | VAL49-VAL69 | |
| A | PHE74-PHE94 | |
| A | LEU105-LEU124 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 29 |
| Details | TOPO_DOM: Lumenal => ECO:0000305|PubMed:12023288, ECO:0000305|PubMed:17632546, ECO:0000305|PubMed:17632548 |
| Chain | Residue | Details |
| A | SER28-ARG48 | |
| A | GLN95-ARG104 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:17632548 |
| Chain | Residue | Details |
| A | ARG31 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:17632548 |
| Chain | Residue | Details |
| A | ARG104 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17632546, ECO:0000269|PubMed:17632548, ECO:0000269|PubMed:27365393 |
| Chain | Residue | Details |
| A | ARG30 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17632548 |
| Chain | Residue | Details |
| A | ARG51 | |
| A | GLU58 | |
| A | TYR93 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by RPS6KB1 => ECO:0000269|PubMed:27365393 |
| Chain | Residue | Details |
| A | SER36 |
