4RYX
Crystal structure of RPE65 in complex with emixustat and palmitate, P6522 crystal form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001523 | biological_process | retinoid metabolic process |
| A | 0001786 | molecular_function | phosphatidylserine binding |
| A | 0001895 | biological_process | retina homeostasis |
| A | 0003834 | molecular_function | beta-carotene 15,15'-dioxygenase activity |
| A | 0004744 | molecular_function | obsolete retinal isomerase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0050908 | biological_process | detection of light stimulus involved in visual perception |
| 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 | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A 601 |
| Chain | Residue |
| A | HIS180 |
| A | HIS241 |
| A | HIS313 |
| A | HIS527 |
| A | PLM602 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PLM A 602 |
| Chain | Residue |
| A | PHE418 |
| A | LEU439 |
| A | PHE442 |
| A | HIS527 |
| A | FE2601 |
| A | A3V603 |
| A | HOH846 |
| A | VAL134 |
| A | HIS180 |
| A | HIS241 |
| A | TYR338 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE A3V A 603 |
| Chain | Residue |
| A | PHE61 |
| A | PHE103 |
| A | VAL134 |
| A | THR147 |
| A | GLU148 |
| A | PLM602 |
| A | HOH975 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 604 |
| Chain | Residue |
| A | ARG33 |
| A | PRO35 |
| A | LEU36 |
| A | TRP37 |
| A | TRP37 |
| A | HIS475 |
| A | MPD606 |
| A | HOH755 |
| A | HOH755 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD A 605 |
| Chain | Residue |
| A | GLU283 |
| A | THR284 |
| A | GLY286 |
| A | TRP402 |
| A | HOH944 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD A 606 |
| Chain | Residue |
| A | ARG33 |
| A | TRP37 |
| A | GLY484 |
| A | VAL485 |
| A | ASN506 |
| A | VAL513 |
| A | SO4604 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD A 607 |
| Chain | Residue |
| A | LEU408 |
| A | PHE409 |
| A | LYS455 |
| A | HOH710 |
| A | HOH834 |
| A | HOH834 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19805034","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q16518","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine; in membrane form","evidences":[{"source":"PubMed","id":"15186777","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
