4F30
Structure of RPE65: P6522 crystal form grown in ammonium phosphate solution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001786 | molecular_function | phosphatidylserine binding |
| A | 0003834 | molecular_function | beta-carotene 15,15'-dioxygenase activity |
| A | 0004744 | molecular_function | obsolete retinal isomerase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0007601 | biological_process | visual perception |
| A | 0016020 | cellular_component | membrane |
| A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0031210 | molecular_function | phosphatidylcholine binding |
| A | 0042572 | biological_process | retinol metabolic process |
| A | 0042574 | biological_process | retinal metabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050251 | molecular_function | retinol isomerase activity |
| A | 0052884 | molecular_function | all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity |
| A | 0052885 | molecular_function | all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity |
| A | 1901612 | molecular_function | cardiolipin binding |
| A | 1901827 | biological_process | zeaxanthin biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE2 A 601 |
| Chain | Residue |
| A | HIS180 |
| A | HIS241 |
| A | HIS313 |
| A | HIS527 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 602 |
| Chain | Residue |
| A | ARG33 |
| A | PRO35 |
| A | LEU36 |
| A | TRP37 |
| A | HIS475 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19805034 |
| Chain | Residue | Details |
| A | HIS180 | |
| A | HIS241 | |
| A | HIS313 | |
| A | HIS527 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:15186777 |
| Chain | Residue | Details |
| A | SER2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q16518 |
| Chain | Residue | Details |
| A | THR101 | |
| A | THR105 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q16518 |
| Chain | Residue | Details |
| A | LYS113 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q16518 |
| Chain | Residue | Details |
| A | SER117 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | LIPID: S-palmitoyl cysteine; in membrane form => ECO:0000269|PubMed:19805034 |
| Chain | Residue | Details |
| A | CYS112 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | LIPID: S-palmitoyl cysteine; in membrane form => ECO:0000269|PubMed:15186777 |
| Chain | Residue | Details |
| A | CYS231 | |
| A | CYS329 | |
| A | CYS330 |
