4ZHK
Crystal structure of RPE65 in complex with MB-002
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 |
| B | 0001786 | molecular_function | phosphatidylserine binding |
| B | 0003834 | molecular_function | beta-carotene 15,15'-dioxygenase activity |
| B | 0004744 | molecular_function | obsolete retinal isomerase activity |
| 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 | 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 | A9V607 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue PG4 A 602 |
| Chain | Residue |
| A | PRO463 |
| A | NA603 |
| A | GLN4 |
| A | VAL459 |
| A | TRP460 |
| A | GLN461 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue NA A 603 |
| Chain | Residue |
| A | GLN461 |
| A | PG4602 |
| A | HOH940 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue PGE A 604 |
| Chain | Residue |
| A | ASP320 |
| A | TYR431 |
| A | THR432 |
| A | LYS453 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue PGE A 605 |
| Chain | Residue |
| A | GLY484 |
| A | ASN506 |
| A | HOH807 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue A8V A 606 |
| Chain | Residue |
| A | PHE61 |
| A | PHE103 |
| A | VAL134 |
| A | THR147 |
| A | GLU148 |
| A | ASN175 |
| A | ASN194 |
| A | TYR239 |
| A | HIS241 |
| A | TYR275 |
| A | TYR338 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue A9V A 607 |
| Chain | Residue |
| A | LEU60 |
| A | HIS241 |
| A | PHE312 |
| A | TYR338 |
| A | GLU417 |
| A | PHE418 |
| A | PHE442 |
| A | VAL524 |
| A | HIS527 |
| A | FE2601 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 B 601 |
| Chain | Residue |
| B | HIS180 |
| B | HIS241 |
| B | HIS313 |
| B | HIS527 |
| B | A9V606 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue PG4 B 602 |
| Chain | Residue |
| B | GLN4 |
| B | VAL459 |
| B | TRP460 |
| B | GLN461 |
| B | PRO463 |
| B | NA603 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue NA B 603 |
| Chain | Residue |
| B | GLN461 |
| B | PG4602 |
| B | HOH958 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue PGE B 604 |
| Chain | Residue |
| B | TYR318 |
| B | ASP320 |
| B | PRO430 |
| B | TYR431 |
| B | LYS453 |
| B | HOH702 |
| site_id | AD3 |
| Number of Residues | 11 |
| Details | binding site for residue A8V B 605 |
| Chain | Residue |
| B | PHE61 |
| B | PHE103 |
| B | VAL134 |
| B | THR147 |
| B | GLU148 |
| B | ASN175 |
| B | ASN194 |
| B | TYR239 |
| B | HIS241 |
| B | TYR275 |
| B | TYR338 |
| site_id | AD4 |
| Number of Residues | 11 |
| Details | binding site for residue A9V B 606 |
| Chain | Residue |
| B | LEU60 |
| B | PHE61 |
| B | HIS241 |
| B | HIS313 |
| B | TYR338 |
| B | GLU417 |
| B | PHE418 |
| B | PHE442 |
| B | VAL524 |
| B | HIS527 |
| B | FE2601 |
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 |
