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4RSE

Crystal structure of RPE65 in complex with MB-001 and palmitate

Functional Information from GO Data
ChainGOidnamespacecontents
A0001786molecular_functionphosphatidylserine binding
A0003834molecular_functionbeta-carotene 15,15'-dioxygenase activity
A0004744molecular_functionobsolete retinal isomerase activity
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
A0043231cellular_componentintracellular membrane-bounded organelle
A0046872molecular_functionmetal ion binding
A0050251molecular_functionretinol isomerase activity
A0050896biological_processresponse to stimulus
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
B0001786molecular_functionphosphatidylserine binding
B0003834molecular_functionbeta-carotene 15,15'-dioxygenase activity
B0004744molecular_functionobsolete retinal isomerase activity
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0007601biological_processvisual perception
B0016020cellular_componentmembrane
B0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B0016787molecular_functionhydrolase activity
B0016853molecular_functionisomerase activity
B0031210molecular_functionphosphatidylcholine binding
B0042572biological_processretinol metabolic process
B0042574biological_processretinal metabolic process
B0042802molecular_functionidentical protein binding
B0043231cellular_componentintracellular membrane-bounded organelle
B0046872molecular_functionmetal ion binding
B0050251molecular_functionretinol isomerase activity
B0050896biological_processresponse to stimulus
B0052884molecular_functionall-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity
B0052885molecular_functionall-trans-retinyl-ester hydrolase, 11-cis retinol forming activity
B1901612molecular_functioncardiolipin binding
B1901827biological_processzeaxanthin biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 601
ChainResidue
AHIS180
AHIS241
AHIS313
AHIS527
APLM602

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLM A 602
ChainResidue
ATYR338
AGLU417
APHE418
ALEU439
APHE442
AVAL524
AHIS527
AFE2601
AA6V603
ALEU60
AVAL134
AHIS241
APHE312

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE A6V A 603
ChainResidue
APHE61
APHE103
AVAL134
ATHR147
AGLU148
AASN194
AHIS241
AILE259
ATYR275
ATYR338
APLM602
AHOH795

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 B 601
ChainResidue
BHIS180
BHIS241
BHIS313
BHIS527
BPLM602

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLM B 602
ChainResidue
BLEU60
BVAL134
BHIS180
BHIS241
BTYR338
BGLU417
BPHE418
BLEU439
BPRO444
BVAL524
BHIS527
BFE2601
BA6V603

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE A6V B 603
ChainResidue
BPHE61
BPHE103
BVAL134
BTHR147
BGLU148
BASN175
BASN194
BILE259
BTYR275
BPLM602
BHOH723

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:19805034
ChainResidueDetails
AHIS180
AHIS241
AHIS313
AHIS527
BHIS180
BHIS241
BHIS313
BHIS527

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:15186777
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q16518
ChainResidueDetails
ATHR101
ATHR105
BTHR101
BTHR105

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q16518
ChainResidueDetails
ALYS113
BLYS113

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q16518
ChainResidueDetails
ASER117
BSER117

site_idSWS_FT_FI6
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine; in membrane form => ECO:0000269|PubMed:19805034
ChainResidueDetails
ACYS112
BCYS112

site_idSWS_FT_FI7
Number of Residues6
DetailsLIPID: S-palmitoyl cysteine; in membrane form => ECO:0000269|PubMed:15186777
ChainResidueDetails
ACYS231
ACYS329
ACYS330
BCYS231
BCYS329
BCYS330

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PDB entries from 2024-04-24

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