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 | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| 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 | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| 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 | 40 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"HAMAP-Rule","id":"MF_03207","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 46 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"34117479","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"HAMAP-Rule","id":"MF_03207","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 74 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"34117479","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"HAMAP-Rule","id":"MF_03207","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 32 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 38 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"HAMAP-Rule","id":"MF_03207","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"HAMAP-Rule","id":"MF_03207","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"HAMAP-Rule","id":"MF_03207","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"HAMAP-Rule","id":"MF_03207","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | Motif: {"description":"HxxHH motif","evidences":[{"source":"PubMed","id":"34117479","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"34117479","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"34117479","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6Y7F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
