5UL5
Crystal structure of RPE65 in complex with MB-004 and palmitate
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 | 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 | 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 |
B | 0001523 | biological_process | retinoid metabolic process |
B | 0001786 | molecular_function | phosphatidylserine binding |
B | 0001895 | biological_process | retina homeostasis |
B | 0003834 | molecular_function | beta-carotene 15,15'-dioxygenase activity |
B | 0004744 | molecular_function | obsolete retinal isomerase activity |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0005886 | cellular_component | plasma membrane |
B | 0006629 | biological_process | lipid metabolic process |
B | 0007601 | biological_process | visual perception |
B | 0016020 | cellular_component | membrane |
B | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0031210 | molecular_function | phosphatidylcholine binding |
B | 0042572 | biological_process | retinol metabolic process |
B | 0042574 | biological_process | retinal metabolic process |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0050251 | molecular_function | retinol isomerase activity |
B | 0050908 | biological_process | detection of light stimulus involved in visual perception |
B | 0052884 | molecular_function | all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity |
B | 0052885 | molecular_function | all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity |
B | 1901612 | molecular_function | cardiolipin binding |
B | 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 | 14 |
Details | binding site for residue PLM A 602 |
Chain | Residue |
A | TYR338 |
A | LEU341 |
A | PHE418 |
A | LEU437 |
A | PHE442 |
A | PRO444 |
A | VAL524 |
A | HIS527 |
A | FE2601 |
A | 8D7603 |
A | LEU60 |
A | VAL134 |
A | HIS180 |
A | HIS241 |
site_id | AC3 |
Number of Residues | 11 |
Details | binding site for residue 8D7 A 603 |
Chain | Residue |
A | PHE61 |
A | PHE103 |
A | VAL134 |
A | THR147 |
A | GLU148 |
A | ASN175 |
A | GLY176 |
A | HIS241 |
A | PHE279 |
A | TYR338 |
A | PLM602 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue NA A 604 |
Chain | Residue |
A | GLN461 |
A | PG6605 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue PG6 A 605 |
Chain | Residue |
A | GLN4 |
A | VAL459 |
A | TRP460 |
A | GLN461 |
A | GLU462 |
A | PRO463 |
A | NA604 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue FE2 B 601 |
Chain | Residue |
B | HIS180 |
B | HIS241 |
B | HIS313 |
B | HIS527 |
B | PLM602 |
site_id | AC7 |
Number of Residues | 14 |
Details | binding site for residue PLM B 602 |
Chain | Residue |
B | LEU60 |
B | VAL134 |
B | HIS180 |
B | HIS241 |
B | TYR338 |
B | GLU417 |
B | PHE418 |
B | LEU437 |
B | PHE442 |
B | PRO444 |
B | VAL524 |
B | HIS527 |
B | FE2601 |
B | 8D7603 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue 8D7 B 603 |
Chain | Residue |
B | PHE61 |
B | PHE103 |
B | VAL134 |
B | THR147 |
B | GLU148 |
B | ASN175 |
B | GLY176 |
B | PHE264 |
B | PHE279 |
B | PLM602 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue PG6 B 604 |
Chain | Residue |
B | GLN4 |
B | VAL459 |
B | TRP460 |
B | GLN461 |
B | PRO463 |
B | NA605 |
B | HOH885 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue NA B 605 |
Chain | Residue |
B | GLN461 |
B | PG6604 |
B | HOH885 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19805034 |
Chain | Residue | Details |
A | HIS180 | |
A | HIS241 | |
A | HIS313 | |
A | HIS527 | |
B | HIS180 | |
B | HIS241 | |
B | HIS313 | |
B | HIS527 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:15186777 |
Chain | Residue | Details |
A | SER2 | |
B | SER2 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q16518 |
Chain | Residue | Details |
A | THR101 | |
A | THR105 | |
B | THR101 | |
B | THR105 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q16518 |
Chain | Residue | Details |
A | LYS113 | |
B | LYS113 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q16518 |
Chain | Residue | Details |
A | SER117 | |
B | SER117 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine; in membrane form => ECO:0000269|PubMed:19805034 |
Chain | Residue | Details |
A | CYS112 | |
B | CYS112 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | LIPID: S-palmitoyl cysteine; in membrane form => ECO:0000269|PubMed:15186777 |
Chain | Residue | Details |
A | CYS231 | |
A | CYS329 | |
A | CYS330 | |
B | CYS231 | |
B | CYS329 | |
B | CYS330 |