2UUI
Crystal structure of Human Leukotriene C4 Synthase
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 | 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 | 0046394 | biological_process | carboxylic acid biosynthetic process |
| 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 A1151 |
| Chain | Residue |
| A | HIS-1 |
| A | HIS1 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI A1152 |
| Chain | Residue |
| A | HIS-4 |
| A | HIS-2 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI A1153 |
| Chain | Residue |
| A | HIS-2 |
| A | HOH2001 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LMT A1154 |
| Chain | Residue |
| A | LMT1155 |
| A | TYR109 |
| A | ARG113 |
| A | TRP116 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LMT A1155 |
| Chain | Residue |
| A | ILE27 |
| A | ARG31 |
| A | ARG104 |
| A | LEU108 |
| A | TYR109 |
| A | TRP116 |
| A | LMT1154 |
| A | PLM1160 |
| A | SO41165 |
| A | HOH2101 |
| A | HOH2102 |
| A | HOH2105 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PLM A1170 |
| Chain | Residue |
| A | PRO132 |
| A | LEU135 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PLM A1171 |
| Chain | Residue |
| A | LEU84 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PLM A1173 |
| Chain | Residue |
| A | LEU14 |
| A | GLY77 |
| A | LEU81 |
| A | LEU84 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PLM A1156 |
| Chain | Residue |
| A | LEU18 |
| A | GLN95 |
| A | HOH2016 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PLM A1157 |
| Chain | Residue |
| A | LEU7 |
| A | PHE130 |
| A | PLM1159 |
| A | PLM1161 |
| A | HOH2087 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PLM A1158 |
| Chain | Residue |
| A | LEU14 |
| A | PHE88 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PLM A1159 |
| Chain | Residue |
| A | LEU13 |
| A | PHE130 |
| A | PLM1157 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PLM A1175 |
| Chain | Residue |
| A | ARG99 |
| A | GLN102 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PLM A1160 |
| Chain | Residue |
| A | LMT1155 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PLM A1161 |
| Chain | Residue |
| A | HIS75 |
| A | GLU76 |
| A | GLY77 |
| A | ARG144 |
| A | PLM1157 |
| A | PLM1162 |
| A | PLM1163 |
| A | HOH2062 |
| A | HOH2064 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PLM A1162 |
| Chain | Residue |
| A | GLU4 |
| A | GLY71 |
| A | ILE72 |
| A | PLM1161 |
| A | PLM1163 |
| A | HOH2008 |
| A | HOH2106 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PLM A1163 |
| Chain | Residue |
| A | HIS0 |
| A | LYS2 |
| A | HIS75 |
| A | ARG136 |
| A | PLM1161 |
| A | PLM1162 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A1164 |
| Chain | Residue |
| A | SER100 |
| A | ALA101 |
| A | GLN102 |
| A | HOH2108 |
| site_id | CC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A1165 |
| Chain | Residue |
| A | ASN55 |
| A | TYR93 |
| A | ARG104 |
| A | LEU108 |
| A | LMT1155 |
| A | HOH2102 |
| A | HOH2109 |
| A | HOH2110 |
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 | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"12023288","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17632546","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 29 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"12023288","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17632546","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"12023288","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17632546","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17632546","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27365393","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by RPS6KB1","evidences":[{"source":"PubMed","id":"27365393","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
