4NTB
Mus Musculus LTC4 synthase in GSH complex form
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 | 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 | 0043295 | molecular_function | glutathione binding |
A | 0044877 | molecular_function | protein-containing complex binding |
A | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NI A 201 |
Chain | Residue |
A | HIS1 |
A | HIS1 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 202 |
Chain | Residue |
A | ARG48 |
A | SER100 |
A | SER100 |
A | ALA101 |
A | ALA101 |
A | GLN102 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE GSH A 203 |
Chain | Residue |
A | ILE27 |
A | ARG30 |
A | PHE50 |
A | ARG51 |
A | GLN53 |
A | ASN55 |
A | GLU58 |
A | TYR59 |
A | TYR93 |
A | TYR97 |
A | ARG104 |
A | LEU108 |
A | SER23 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PLM A 204 |
Chain | Residue |
A | LYS2 |
A | VAL128 |
A | PRO132 |
A | LEU135 |
A | ARG136 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PLM A 205 |
Chain | Residue |
A | LEU7 |
A | THR10 |
A | LEU127 |
A | PHE130 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PLM A 206 |
Chain | Residue |
A | LEU18 |
A | GLN95 |
Functional Information from PROSITE/UniProt
site_id | PS01297 |
Number of Residues | 15 |
Details | FLAP_GST2_LTC4S FLAP/GST2/LTC4S family signature. GppeFERVFrAQvNC |
Chain | Residue | Details |
A | GLY42-CYS56 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 79 |
Details | TRANSMEM: Helical => ECO:0000250|UniProtKB:Q16873 |
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:0000250|UniProtKB:Q16873 |
Chain | Residue | Details |
A | SER28-ARG48 | |
A | GLN95-ARG104 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:Q16873 |
Chain | Residue | Details |
A | ALA70-PHE73 | |
A | GLY125-ALA150 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q16873 |
Chain | Residue | Details |
A | ARG31 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q16873 |
Chain | Residue | Details |
A | ARG104 |
site_id | SWS_FT_FI6 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q16873 |
Chain | Residue | Details |
A | GLN53 | |
A | GLU58 | |
A | TYR93 | |
A | ARG30 | |
A | ARG51 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q16873 |
Chain | Residue | Details |
A | SER36 |