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4F2Z

Crystal structure of RPE65 in a lipid environment

Functional Information from GO Data
ChainGOidnamespacecontents
A0001523biological_processretinoid metabolic process
A0001786molecular_functionphosphatidylserine binding
A0001895biological_processretina homeostasis
A0003834molecular_functionbeta-carotene 15,15'-dioxygenase activity
A0004744molecular_functionobsolete retinal isomerase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0007601biological_processvisual perception
A0016020cellular_componentmembrane
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0016787molecular_functionhydrolase activity
A0016853molecular_functionisomerase activity
A0031210molecular_functionphosphatidylcholine binding
A0042572biological_processretinol metabolic process
A0042574biological_processretinal metabolic process
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0050251molecular_functionretinol isomerase activity
A0050908biological_processdetection of light stimulus involved in visual perception
A0052884molecular_functionall-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity
A0052885molecular_functionall-trans-retinyl-ester hydrolase, 11-cis retinol forming activity
A1901612molecular_functioncardiolipin binding
A1901827biological_processzeaxanthin biosynthetic process
E0001523biological_processretinoid metabolic process
E0001786molecular_functionphosphatidylserine binding
E0001895biological_processretina homeostasis
E0003834molecular_functionbeta-carotene 15,15'-dioxygenase activity
E0004744molecular_functionobsolete retinal isomerase activity
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005783cellular_componentendoplasmic reticulum
E0005789cellular_componentendoplasmic reticulum membrane
E0005886cellular_componentplasma membrane
E0006629biological_processlipid metabolic process
E0007601biological_processvisual perception
E0016020cellular_componentmembrane
E0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
E0016787molecular_functionhydrolase activity
E0016853molecular_functionisomerase activity
E0031210molecular_functionphosphatidylcholine binding
E0042572biological_processretinol metabolic process
E0042574biological_processretinal metabolic process
E0042802molecular_functionidentical protein binding
E0046872molecular_functionmetal ion binding
E0050251molecular_functionretinol isomerase activity
E0050908biological_processdetection of light stimulus involved in visual perception
E0052884molecular_functionall-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity
E0052885molecular_functionall-trans-retinyl-ester hydrolase, 11-cis retinol forming activity
E1901612molecular_functioncardiolipin binding
E1901827biological_processzeaxanthin biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 A 601
ChainResidue
AHIS180
AHIS241
AHIS313
AHIS527

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 E 601
ChainResidue
EHIS180
EHIS241
EHIS313
EHIS527

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:19805034
ChainResidueDetails
AHIS180
AHIS241
AHIS313
AHIS527
EHIS180
EHIS241
EHIS313
EHIS527

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:15186777
ChainResidueDetails
ASER2
ESER2

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q16518
ChainResidueDetails
ATHR101
ATHR105
ETHR101
ETHR105

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q16518
ChainResidueDetails
ALYS113
ELYS113

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q16518
ChainResidueDetails
ASER117
ESER117

site_idSWS_FT_FI6
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine; in membrane form => ECO:0000269|PubMed:19805034
ChainResidueDetails
ACYS112
ECYS112

site_idSWS_FT_FI7
Number of Residues6
DetailsLIPID: S-palmitoyl cysteine; in membrane form => ECO:0000269|PubMed:15186777
ChainResidueDetails
ACYS231
ACYS329
ACYS330
ECYS231
ECYS329
ECYS330

227111

PDB entries from 2024-11-06

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