4JRZ
Human LTC4 synthase in complex with product analogs - implications for enzyme catalysis
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 201 |
Chain | Residue |
A | HIS-1 |
A | HIS-1 |
A | HIS-1 |
A | HIS1 |
A | HIS1 |
A | HIS1 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NI A 202 |
Chain | Residue |
A | HIS-4 |
A | HIS-4 |
A | HIS-2 |
A | HIS-4 |
A | HIS-2 |
A | HIS-2 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NI A 203 |
Chain | Residue |
A | HIS-1 |
A | HIS-2 |
A | HIS-3 |
A | HOH317 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 204 |
Chain | Residue |
A | SER100 |
A | SER100 |
A | ALA101 |
A | ALA101 |
A | GLN102 |
A | GLN102 |
A | HOH301 |
A | HOH301 |
A | HOH303 |
A | HOH303 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PAM A 205 |
Chain | Residue |
A | HIS0 |
A | HIS1 |
A | LYS2 |
A | GLU4 |
A | TRP68 |
A | ILE72 |
A | HOH310 |
A | HOH314 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PLM A 206 |
Chain | Residue |
A | PHE74 |
A | ALA128 |
A | LEU135 |
A | ARG136 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PLM A 207 |
Chain | Residue |
A | LEU127 |
A | PHE130 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PLM A 208 |
Chain | Residue |
A | TYR21 |
A | GLN95 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PLM A 209 |
Chain | Residue |
A | LEU81 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PLM A 210 |
Chain | Residue |
A | LEU131 |
site_id | BC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE GTX A 211 |
Chain | Residue |
A | SER23 |
A | VAL26 |
A | ILE27 |
A | ARG30 |
A | TYR50 |
A | GLN53 |
A | ASN55 |
A | GLU58 |
A | TYR59 |
A | TYR93 |
A | ARG104 |
A | LEU108 |
A | ALA112 |
A | PHE116 |
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 |