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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8U4E

Cryo-EM structure of long form insulin receptor (IR-B) with three IGF2 bound, asymmetric conformation.

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGnardiikgeaetr.....VAVK
ChainResidueDetails
ALEU1002-LYS1030
site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV
ChainResidueDetails
APHE1128-VAL1140
site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR
ChainResidueDetails
AASP1156-ARG1164
site_idPS00262
Number of Residues15
DetailsINSULIN Insulin family signature. CCFRsCDlalLetyC
ChainResidueDetails
CCYS46-CYS60
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsSITE: Important for interaction with integrin => ECO:0000269|PubMed:28873464
ChainResidueDetails
CARG37
CARG24
EARG34
EARG37
EARG38
CARG34
CARG38
DARG24
DARG34
DARG37
DARG38
EARG24
site_idSWS_FT_FI2
Number of Residues3
DetailsCARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360
ChainResidueDetails
ETHR72
CTHR72
DTHR72
site_idSWS_FT_FI3
Number of Residues3
DetailsCARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:1569071, ECO:0000269|PubMed:22171320
ChainResidueDetails
ETHR75
CTHR75
DTHR75
site_idSWS_FT_FI4
Number of Residues3
DetailsCARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320
ChainResidueDetails
ETHR139
CTHR139
DTHR139
site_idSWS_FT_FI5
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056
ChainResidueDetails
AGLU1077
ASER1006
BASP1150
ALYS1030
AARG1136
AASP1150
BSER1006
BLYS1030
BGLU1077
BARG1136
site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Insulin-binding => ECO:0000305
ChainResidueDetails
APHE39
BPHE39
site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
BSER373
ASER373
ASER380
BSER380
site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ATYR374
BTYR374
site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305
ChainResidueDetails
ATYR984
BTYR965
ATYR965
BTYR984
site_idSWS_FT_FI10
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:3166375
ChainResidueDetails
ATYR1334
ATYR972
ATYR1328
BTYR972
BTYR1328
BTYR1334
site_idSWS_FT_FI11
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016
ChainResidueDetails
ATYR1163
ATYR1158
ATYR1162
BTYR1158
BTYR1162
BTYR1163
site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:23302862, ECO:0000269|PubMed:2983222
ChainResidueDetails
AASN16
BASN16
site_idSWS_FT_FI13
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:23302862
ChainResidueDetails
AASN255
AASN25
AASN111
BASN25
BASN111
BASN255
site_idSWS_FT_FI14
Number of Residues14
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN606
AASN78
BASN606
BASN624
BASN671
BASN755
BASN906
AASN295
AASN624
AASN671
AASN755
AASN906
BASN78
BASN295
site_idSWS_FT_FI15
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23302862
ChainResidueDetails
AASN215
BASN215
site_idSWS_FT_FI16
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147
ChainResidueDetails
BASN337
AASN337
AASN397
BASN397
site_idSWS_FT_FI17
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:19349973
ChainResidueDetails
AASN418
BASN418
site_idSWS_FT_FI18
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1472036, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN514
BASN514
site_idSWS_FT_FI19
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2983222
ChainResidueDetails
AASN742
BASN742
site_idSWS_FT_FI20
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
AASN893
BASN893
Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 246
ChainResidueDetails
AASN1137metal ligand
AASP1132increase nucleophilicity, proton acceptor, proton donor, steric role
AASP1150metal ligand
AARG1136electrostatic stabiliser, increase electrophilicity, promote heterolysis
site_idMCSA2
Number of Residues4
DetailsM-CSA 246
ChainResidueDetails
BASN1137metal ligand
BASP1132increase nucleophilicity, proton acceptor, proton donor, steric role
BARG1136electrostatic stabiliser, increase electrophilicity, promote heterolysis
BASP1150metal ligand

219869

PDB entries from 2024-05-15

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