Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue NAP A 401 |
| Chain | Residue |
| A | PHE90 |
| A | LYS225 |
| A | TYR240 |
| A | HIS241 |
| A | PRO263 |
| A | TYR285 |
| A | ALA288 |
| A | LEU291 |
| A | PHE326 |
| A | HIS327 |
| A | LEU328 |
| A | ASN172 |
| A | MET374 |
| A | LYS377 |
| A | ASN379 |
| A | HOH502 |
| A | THR175 |
| A | MET196 |
| A | GLY199 |
| A | GLY200 |
| A | VAL201 |
| A | ALA221 |
| A | SER222 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | binding site for residue NAP B 401 |
| Chain | Residue |
| B | PHE90 |
| B | VAL171 |
| B | THR175 |
| B | MET196 |
| B | GLY199 |
| B | GLY200 |
| B | VAL201 |
| B | ALA221 |
| B | SER222 |
| B | LYS225 |
| B | TYR240 |
| B | HIS241 |
| B | PRO263 |
| B | TYR285 |
| B | ALA288 |
| B | LEU291 |
| B | PHE326 |
| B | HIS327 |
| B | LEU328 |
| B | GLN375 |
| B | LYS377 |
| B | ASN379 |
| B | HOH503 |
| B | HOH504 |
| B | HOH509 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | binding site for residue NAP C 401 |
| Chain | Residue |
| C | PHE90 |
| C | VAL171 |
| C | ASN172 |
| C | THR175 |
| C | MET196 |
| C | GLY199 |
| C | GLY200 |
| C | VAL201 |
| C | ALA221 |
| C | SER222 |
| C | LYS225 |
| C | TYR240 |
| C | HIS241 |
| C | TYR285 |
| C | ALA288 |
| C | LEU291 |
| C | PHE326 |
| C | HIS327 |
| C | LEU328 |
| C | MET374 |
| C | GLN375 |
| C | LYS377 |
| C | ASN379 |
| C | HOH502 |
| C | HOH505 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue NAP D 401 |
| Chain | Residue |
| D | PHE90 |
| D | THR175 |
| D | MET196 |
| D | GLY199 |
| D | GLY200 |
| D | VAL201 |
| D | ALA221 |
| D | SER222 |
| D | LYS225 |
| D | TYR240 |
| D | HIS241 |
| D | TYR285 |
| D | LEU291 |
| D | PHE326 |
| D | HIS327 |
| D | LEU328 |
| D | GLN375 |
| D | LYS377 |
| D | ASN379 |
| D | HOH503 |
| D | HOH505 |
| D | HOH509 |
Functional Information from PROSITE/UniProt
| site_id | PS01162 |
| Number of Residues | 22 |
| Details | QOR_ZETA_CRYSTAL Quinone oxidoreductase / zeta-crystallin signature. GHsvLvhmAAGGvGmaavQlcR |
| Chain | Residue | Details |
| A | GLY189-ARG210 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | Region: {"description":"Extruded flexible loop; potentially involved in lipid transfer and membrane binding","evidences":[{"source":"PubMed","id":"32005660","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Motif: {"description":"Required for negative regulation of mitochondrial fusion","evidences":[{"source":"UniProtKB","id":"Q3MIE4","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 52 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33483563","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6LHR","evidenceCode":"ECO:0007744"}]} |
6LHR
