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8EM7

Cryo-EM structure of LRP2 at pH 5.2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
B0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CvNmrgsFrCaC
ChainResidueDetails
ACYS1405-CYS1416
ACYS3128-CYS3139
ACYS3169-CYS3180
ACYS4023-CYS4034

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CkCssGysGEyC
ChainResidueDetails
ACYS4401-CYS4412

site_idPS00615
Number of Residues27
DetailsC_TYPE_LECTIN_1 C-type lectin domain signature. CVdidecketpq..LCSQKCenvigsYIC
ChainResidueDetails
ACYS3152-CYS3178

site_idPS01186
Number of Residues15
DetailsEGF_2 EGF-like domain signature 2. ClCeeGYilergqh.C
ChainResidueDetails
ACYS370-CYS384
ACYS688-CYS703
ACYS1374-CYS1389
ACYS1726-CYS1741
ACYS2044-CYS2059
ACYS3137-CYS3152
ACYS3178-CYS3193
ACYS4401-CYS4412

site_idPS01187
Number of Residues24
DetailsEGF_CA Calcium-binding EGF-like domain signature. DvNECdipgf.........Csqh....CvNmrgsFrC
ChainResidueDetails
AASP1391-CYS1414
AASP3154-CYS3178
AASP4009-CYS4032

site_idPS01209
Number of Residues23
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIpaswr.CDgtrDCldd.TDEig...C
ChainResidueDetails
ACYS40-CYS62
ACYS1201-CYS1223
ACYS1244-CYS1267
ACYS1284-CYS1306
ACYS1326-CYS1349
ACYS2713-CYS2737
ACYS2754-CYS2776
ACYS2836-CYS2860
ACYS2878-CYS2901
ACYS2920-CYS2945
ACYS3007-CYS3029
ACYS80-CYS103
ACYS3046-CYS3070
ACYS3089-CYS3111
ACYS3527-CYS3550
ACYS3608-CYS3632
ACYS3649-CYS3673
ACYS3694-CYS3716
ACYS3734-CYS3756
ACYS3773-CYS3795
ACYS3812-CYS3834
ACYS3856-CYS3880
ACYS120-CYS142
ACYS3898-CYS3922
ACYS3942-CYS3964
ACYS195-CYS217
ACYS234-CYS256
ACYS1037-CYS1059
ACYS1079-CYS1101
ACYS1122-CYS1144
ACYS1162-CYS1184

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8798
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AGLN26-THR4425
BGLN26-THR4425

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AMET4426-PHE4446
BMET4426-PHE4446

site_idSWS_FT_FI3
Number of Residues426
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
APHE4447-VAL4660
BPHE4447-VAL4660

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P98164
ChainResidueDetails
ATRP1127
BASP1134
BASP1140
BGLU1141
AASP1130
AASP1132
AASP1134
AASP1140
AGLU1141
BTRP1127
BASP1130
BASP1132

site_idSWS_FT_FI5
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P98158
ChainResidueDetails
ATYR1206
BASP1213
BASP1219
BGLU1220
AASP1209
AVAL1211
AASP1213
AASP1219
AGLU1220
BTYR1206
BASP1209
BVAL1211

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER4464
ASER4467
ASER4577
ASER4658
BSER4464
BSER4467
BSER4577
BSER4658

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P98158
ChainResidueDetails
ASER4624
BSER4624

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ATHR4637
BTHR4637

site_idSWS_FT_FI9
Number of Residues84
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN159
AASN1328
AASN1341
AASN1384
AASN1451
AASN1497
AASN1551
AASN1676
AASN1733
AASN1811
AASN2131
AASN178
AASN2134
AASN2178
AASN2225
AASN2396
AASN2488
AASN2548
AASN2782
AASN2810
AASN2949
AASN2989
AASN299
AASN3127
AASN3213
AASN3259
AASN3317
AASN3357
AASN3448
AASN3566
AASN3682
AASN3840
AASN3969
AASN340
AASN3980
AASN4070
AASN4329
BASN159
BASN178
BASN299
BASN340
BASN462
BASN657
BASN865
AASN462
BASN1063
BASN1187
BASN1328
BASN1341
BASN1384
BASN1451
BASN1497
BASN1551
BASN1676
BASN1733
AASN657
BASN1811
BASN2131
BASN2134
BASN2178
BASN2225
BASN2396
BASN2488
BASN2548
BASN2782
BASN2810
AASN865
BASN2949
BASN2989
BASN3127
BASN3213
BASN3259
BASN3317
BASN3357
BASN3448
BASN3566
BASN3682
AASN1063
BASN3840
BASN3969
BASN3980
BASN4070
BASN4329
AASN1187

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
AASN387
BASN387

227111

PDB entries from 2024-11-06

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