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8YYT

Cryo-EM structure of the complex IR with four insulin

Functional Information from GO Data
ChainGOidnamespacecontents
C0005179molecular_functionhormone activity
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0006006biological_processglucose metabolic process
C0007165biological_processsignal transduction
C0042593biological_processglucose homeostasis
C0050714biological_processpositive regulation of protein secretion
C1901701biological_processcellular response to oxygen-containing compound
D0005179molecular_functionhormone activity
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0006006biological_processglucose metabolic process
D0007165biological_processsignal transduction
D0042593biological_processglucose homeostasis
D0050714biological_processpositive regulation of protein secretion
D1901701biological_processcellular response to oxygen-containing compound
E0005179molecular_functionhormone activity
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0006006biological_processglucose metabolic process
E0007165biological_processsignal transduction
E0042593biological_processglucose homeostasis
E0050714biological_processpositive regulation of protein secretion
E1901701biological_processcellular response to oxygen-containing compound
F0005179molecular_functionhormone activity
F0005576cellular_componentextracellular region
F0005615cellular_componentextracellular space
F0006006biological_processglucose metabolic process
F0007165biological_processsignal transduction
F0042593biological_processglucose homeostasis
F0050714biological_processpositive regulation of protein secretion
F1901701biological_processcellular response to oxygen-containing compound
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGnardiikgeaetr.....VAVK
ChainResidueDetails
ALEU1017-LYS1045

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV
ChainResidueDetails
APHE1143-VAL1155

site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR
ChainResidueDetails
AASP1171-ARG1179

site_idPS00262
Number of Residues15
DetailsINSULIN Insulin family signature. CCTSiCSlyqLenyC
ChainResidueDetails
CCYS36-CYS50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1846
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AHIS28-VAL758
APRO763-PHE956
BHIS28-VAL758
BPRO763-PHE956

site_idSWS_FT_FI2
Number of Residues44
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
ASER957-LEU979
BSER957-LEU979

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9312016
ChainResidueDetails
APHE1159
BPHE1159

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056
ChainResidueDetails
AILE1033
BTYR1177
AILE1057
AARG1104
AILE1163
ATYR1177
BILE1033
BILE1057
BARG1104
BILE1163

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Insulin-binding => ECO:0000305
ChainResidueDetails
APHE66
BPHE66

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER400
ASER407
BSER400
BSER407

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ATYR401
BTYR401

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305
ChainResidueDetails
AASP992
AILE1011
BASP992
BILE1011

site_idSWS_FT_FI9
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:3166375
ChainResidueDetails
ATYR999
AGLY1355
AILE1361
BTYR999
BGLY1355
BILE1361

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:38056462
ChainResidueDetails
ALYS1083
BLYS1083

site_idSWS_FT_FI11
Number of Residues4
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:26584640, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016
ChainResidueDetails
ALEU1185
ATRP1190
BLEU1185
BTRP1190

site_idSWS_FT_FI12
Number of Residues2
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
AARG1189
BARG1189

site_idSWS_FT_FI13
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:23302862, ECO:0000269|PubMed:2983222
ChainResidueDetails
AASN43
BASN43

site_idSWS_FT_FI14
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:23302862
ChainResidueDetails
AASN52
AASN138
AASN282
BASN52
BASN138
BASN282

site_idSWS_FT_FI15
Number of Residues14
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN105
BASN633
BASN651
BASN698
BGLU782
BTHR933
AASN322
AASN633
AASN651
AASN698
AGLU782
ATHR933
BASN105
BASN322

site_idSWS_FT_FI16
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23302862
ChainResidueDetails
AASN242
BASN242

site_idSWS_FT_FI17
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147
ChainResidueDetails
AASN364
AASN424
BASN364
BASN424

site_idSWS_FT_FI18
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:19349973
ChainResidueDetails
AASN445
BASN445

site_idSWS_FT_FI19
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1472036, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN541
BASN541

site_idSWS_FT_FI20
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2983222
ChainResidueDetails
APRO769
BPRO769

site_idSWS_FT_FI21
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
AGLY920
BGLY920

site_idSWS_FT_FI22
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27577745
ChainResidueDetails
AGLY1079
BGLY1079

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 246
ChainResidueDetails

site_idMCSA2
Number of Residues
DetailsM-CSA 246
ChainResidueDetails

237992

PDB entries from 2025-06-25

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