6Y7F
Crystal structure of human ELOVL fatty acid elongase 7 (ELOVL7)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0006636 | biological_process | unsaturated fatty acid biosynthetic process |
| A | 0009922 | molecular_function | fatty acid elongase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019367 | biological_process | fatty acid elongation, saturated fatty acid |
| A | 0030148 | biological_process | sphingolipid biosynthetic process |
| A | 0030497 | biological_process | fatty acid elongation |
| A | 0034625 | biological_process | fatty acid elongation, monounsaturated fatty acid |
| A | 0034626 | biological_process | fatty acid elongation, polyunsaturated fatty acid |
| A | 0035338 | biological_process | long-chain fatty-acyl-CoA biosynthetic process |
| A | 0042761 | biological_process | very long-chain fatty acid biosynthetic process |
| B | 0005515 | molecular_function | protein binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0006636 | biological_process | unsaturated fatty acid biosynthetic process |
| B | 0009922 | molecular_function | fatty acid elongase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019367 | biological_process | fatty acid elongation, saturated fatty acid |
| B | 0030148 | biological_process | sphingolipid biosynthetic process |
| B | 0030497 | biological_process | fatty acid elongation |
| B | 0034625 | biological_process | fatty acid elongation, monounsaturated fatty acid |
| B | 0034626 | biological_process | fatty acid elongation, polyunsaturated fatty acid |
| B | 0035338 | biological_process | long-chain fatty-acyl-CoA biosynthetic process |
| B | 0042761 | biological_process | very long-chain fatty acid biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 36 |
| Details | binding site for residue OFN A 301 |
| Chain | Residue |
| A | MET68 |
| A | GLN142 |
| A | HIS147 |
| A | HIS150 |
| A | TRP158 |
| A | GLY161 |
| A | ASN177 |
| A | HIS181 |
| A | MET184 |
| A | TYR187 |
| A | TYR188 |
| A | TYR71 |
| A | SER191 |
| A | GLN198 |
| A | LYS204 |
| A | LEU207 |
| A | THR208 |
| A | GLN211 |
| A | PHE215 |
| A | TYR245 |
| A | PHE253 |
| A | PHE256 |
| A | ASN72 |
| A | ARG266 |
| A | HOH407 |
| A | HOH410 |
| A | HOH414 |
| A | HOH424 |
| A | HOH429 |
| A | HOH440 |
| A | LYS124 |
| A | ASP130 |
| A | PHE133 |
| A | PHE134 |
| A | ARG137 |
| A | LYS139 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue 37X A 302 |
| Chain | Residue |
| A | TYR197 |
| A | TYR200 |
| A | 37X303 |
| A | HOH409 |
| A | HOH417 |
| A | HOH433 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue 37X A 303 |
| Chain | Residue |
| A | LEU190 |
| A | 37X302 |
| A | 37X304 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue 37X A 304 |
| Chain | Residue |
| A | TYR200 |
| A | TRP202 |
| A | TRP203 |
| A | TYR206 |
| A | 37X303 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 305 |
| Chain | Residue |
| A | ARG259 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue 37X B 302 |
| Chain | Residue |
| A | TYR81 |
| A | LEU119 |
| B | PRO23 |
| B | GLU26 |
| B | ARG106 |
| B | HOH418 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 303 |
| Chain | Residue |
| B | ARG259 |
| B | HOH423 |
| site_id | AC8 |
| Number of Residues | 41 |
| Details | binding site for Di-peptide OFN B 301 and HIS B 181 |
| Chain | Residue |
| B | HOH433 |
| B | MET68 |
| B | TYR71 |
| B | ASN72 |
| B | LYS124 |
| B | GLU127 |
| B | ASP130 |
| B | PHE133 |
| B | PHE134 |
| B | ARG137 |
| B | LYS139 |
| B | GLN142 |
| B | HIS147 |
| B | HIS150 |
| B | GLY161 |
| B | ASN177 |
| B | THR178 |
| B | ALA179 |
| B | VAL180 |
| B | VAL182 |
| B | VAL183 |
| B | MET184 |
| B | TYR185 |
| B | TYR187 |
| B | TYR188 |
| B | SER191 |
| B | ALA192 |
| B | GLN198 |
| B | LYS204 |
| B | LEU207 |
| B | THR208 |
| B | GLN211 |
| B | PHE215 |
| B | TYR245 |
| B | PHE253 |
| B | PHE256 |
| B | ARG266 |
| B | HOH406 |
| B | HOH407 |
| B | HOH417 |
| B | HOH426 |
| site_id | AC9 |
| Number of Residues | 42 |
| Details | binding site for Di-peptide OFN B 301 and HIS B 150 |
| Chain | Residue |
| B | MET68 |
| B | TYR71 |
| B | ASN72 |
| B | LYS124 |
| B | ASP130 |
| B | PHE133 |
| B | PHE134 |
| B | ARG137 |
| B | LYS139 |
| B | GLN142 |
| B | LEU146 |
| B | HIS147 |
| B | VAL148 |
| B | PHE149 |
| B | HIS151 |
| B | THR152 |
| B | ILE153 |
| B | MET154 |
| B | GLY161 |
| B | ASN177 |
| B | HIS181 |
| B | MET184 |
| B | TYR187 |
| B | TYR188 |
| B | SER191 |
| B | ALA192 |
| B | GLN198 |
| B | LYS204 |
| B | LEU207 |
| B | THR208 |
| B | GLN211 |
| B | PHE215 |
| B | TYR245 |
| B | PHE249 |
| B | PHE253 |
| B | PHE256 |
| B | ARG266 |
| B | HOH406 |
| B | HOH407 |
| B | HOH417 |
| B | HOH426 |
| B | HOH433 |
Functional Information from PROSITE/UniProt
| site_id | PS01188 |
| Number of Residues | 9 |
| Details | ELO ELO family signature. VtFLHVFHH |
| Chain | Residue | Details |
| A | VAL143-HIS151 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 124 |
| Details | TOPO_DOM: Lumenal => ECO:0000305|PubMed:34117479 |
| Chain | Residue | Details |
| A | ALA2-ASP27 | |
| A | GLY94-ARG115 | |
| A | LYS163-THR171 | |
| A | MET228-PRO236 | |
| B | ALA2-ASP27 | |
| B | GLY94-ARG115 | |
| B | LYS163-THR171 | |
| B | MET228-PRO236 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000255|HAMAP-Rule:MF_03207 |
| Chain | Residue | Details |
| A | TRP28-VAL48 | |
| B | TRP28-VAL48 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 92 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:34117479 |
| Chain | Residue | Details |
| A | THR49-ASN72 | |
| A | TYR258-ASN281 | |
| B | THR49-ASN72 | |
| B | TYR258-ASN281 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000255|HAMAP-Rule:MF_03207 |
| Chain | Residue | Details |
| A | PHE73-ILE93 | |
| B | PHE73-ILE93 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000255|HAMAP-Rule:MF_03207 |
| Chain | Residue | Details |
| A | THR116-LEU136 | |
| B | THR116-LEU136 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 32 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
| Chain | Residue | Details |
| A | ARG137-GLN142 | |
| A | PRO195-TYR206 | |
| B | ARG137-GLN142 | |
| B | PRO195-TYR206 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 38 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000255|HAMAP-Rule:MF_03207 |
| Chain | Residue | Details |
| A | VAL143-VAL162 | |
| B | VAL143-VAL162 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 44 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000255|HAMAP-Rule:MF_03207 |
| Chain | Residue | Details |
| A | PHE172-GLY194 | |
| B | PHE172-GLY194 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000255|HAMAP-Rule:MF_03207 |
| Chain | Residue | Details |
| A | LEU207-PHE227 | |
| B | LEU207-PHE227 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000255|HAMAP-Rule:MF_03207 |
| Chain | Residue | Details |
| A | VAL237-TRP257 | |
| B | VAL237-TRP257 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:34117479 |
| Chain | Residue | Details |
| A | HIS150 | |
| B | HIS150 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:34117479, ECO:0007744|PDB:6Y7F |
| Chain | Residue | Details |
| A | LYS124 | |
| A | ARG266 | |
| B | LYS124 | |
| B | ARG137 | |
| B | LYS139 | |
| B | GLN142 | |
| B | HIS147 | |
| B | TYR187 | |
| B | LYS204 | |
| B | THR208 | |
| B | GLN211 | |
| A | ARG137 | |
| B | ARG266 | |
| A | LYS139 | |
| A | GLN142 | |
| A | HIS147 | |
| A | TYR187 | |
| A | LYS204 | |
| A | THR208 | |
| A | GLN211 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:34117479 |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 |
