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5UL5

Crystal structure of RPE65 in complex with MB-004 and palmitate

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
B0001523biological_processretinoid metabolic process
B0001786molecular_functionphosphatidylserine binding
B0001895biological_processretina homeostasis
B0003834molecular_functionbeta-carotene 15,15'-dioxygenase activity
B0004744molecular_functionobsolete retinal isomerase activity
B0005634cellular_componentnucleus
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
B0046872molecular_functionmetal ion binding
B0050251molecular_functionretinol isomerase activity
B0050908biological_processdetection of light stimulus involved in visual perception
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 Residues14
Detailsbinding site for residue PLM A 602
ChainResidue
ATYR338
ALEU341
APHE418
ALEU437
APHE442
APRO444
AVAL524
AHIS527
AFE2601
A8D7603
ALEU60
AVAL134
AHIS180
AHIS241

site_idAC3
Number of Residues11
Detailsbinding site for residue 8D7 A 603
ChainResidue
APHE61
APHE103
AVAL134
ATHR147
AGLU148
AASN175
AGLY176
AHIS241
APHE279
ATYR338
APLM602

site_idAC4
Number of Residues2
Detailsbinding site for residue NA A 604
ChainResidue
AGLN461
APG6605

site_idAC5
Number of Residues7
Detailsbinding site for residue PG6 A 605
ChainResidue
AGLN4
AVAL459
ATRP460
AGLN461
AGLU462
APRO463
ANA604

site_idAC6
Number of Residues5
Detailsbinding site for residue FE2 B 601
ChainResidue
BHIS180
BHIS241
BHIS313
BHIS527
BPLM602

site_idAC7
Number of Residues14
Detailsbinding site for residue PLM B 602
ChainResidue
BLEU60
BVAL134
BHIS180
BHIS241
BTYR338
BGLU417
BPHE418
BLEU437
BPHE442
BPRO444
BVAL524
BHIS527
BFE2601
B8D7603

site_idAC8
Number of Residues10
Detailsbinding site for residue 8D7 B 603
ChainResidue
BPHE61
BPHE103
BVAL134
BTHR147
BGLU148
BASN175
BGLY176
BPHE264
BPHE279
BPLM602

site_idAC9
Number of Residues7
Detailsbinding site for residue PG6 B 604
ChainResidue
BGLN4
BVAL459
BTRP460
BGLN461
BPRO463
BNA605
BHOH885

site_idAD1
Number of Residues3
Detailsbinding site for residue NA B 605
ChainResidue
BGLN461
BPG6604
BHOH885

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

227933

PDB entries from 2024-11-27

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