2UUH
Crystal structure of Human Leukotriene C4 Synthase in complex with substrate glutathione
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 | 6 |
| Details | BINDING SITE FOR RESIDUE NI A 1147 |
| Chain | Residue |
| A | HIS-4 |
| A | HIS-4 |
| A | HIS-4 |
| A | HIS-2 |
| A | HIS-2 |
| A | HIS-2 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI A 1148 |
| Chain | Residue |
| A | HIS1 |
| A | HIS1 |
| A | HIS1 |
| A | HIS-1 |
| A | HIS-1 |
| A | HIS-1 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PLM A 1152 |
| Chain | Residue |
| A | ALA128 |
| A | LEU135 |
| A | HOH2013 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PLM A 1153 |
| Chain | Residue |
| A | PHE130 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PLM A 1154 |
| Chain | Residue |
| A | GLN95 |
| A | HOH2086 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PLM A 1156 |
| Chain | Residue |
| A | HOH2077 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE LMU A 1149 |
| Chain | Residue |
| A | ILE27 |
| A | ARG30 |
| A | ARG31 |
| A | SER36 |
| A | PRO37 |
| A | TYR59 |
| A | GLN102 |
| A | ARG104 |
| A | LEU105 |
| A | TYR109 |
| A | ALA112 |
| A | TRP116 |
| A | GSH1150 |
| A | HOH2036 |
| A | HOH2063 |
| A | HOH2119 |
| A | HOH2121 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE GSH A 1150 |
| Chain | Residue |
| A | SER23 |
| A | ILE27 |
| A | ARG30 |
| A | PRO37 |
| A | TYR50 |
| A | ARG51 |
| A | GLN53 |
| A | ASN55 |
| A | GLU58 |
| A | TYR59 |
| A | TYR93 |
| A | TYR97 |
| A | ARG104 |
| A | LEU108 |
| A | LMU1149 |
| A | HOH2069 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PAM A 1151 |
| Chain | Residue |
| A | GLU4 |
| A | TRP68 |
| A | ILE72 |
| A | HOH2120 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1155 |
| Chain | Residue |
| A | ARG48 |
| A | SER100 |
| A | SER100 |
| A | ALA101 |
| A | ALA101 |
| A | GLN102 |
| A | GLN102 |
| A | HOH2121 |
| A | HOH2122 |
| A | HOH2122 |
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 | 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_FI2 |
| 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_FI3 |
| Number of Residues | 28 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:12023288, ECO:0000305|PubMed:17632546, ECO:0000305|PubMed:17632548 |
| Chain | Residue | Details |
| A | ALA70-PHE73 | |
| A | GLY125-ALA150 |
| 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 |
