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1GAG

CRYSTAL STRUCTURE OF THE INSULIN RECEPTOR KINASE IN COMPLEX WITH A BISUBSTRATE INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 201
ChainResidue
AASN1137
AASP1150
BHOH1
B112101

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
AHOH21
AHOH22
AASP1150
BHOH20
B112101

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 112 B 101
ChainResidue
AMG201
AMG202
ALEU1002
AGLY1005
ASER1006
AVAL1010
AALA1028
ALYS1030
AGLU1077
AMET1079
AASP1083
AASP1132
AARG1136
AASN1137
AASP1150
BHOH1
BHOH14
BHOH20
BPRO102
BALA103
BPHE107

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR CHAIN B OF BISUBSTRATE PEPTIDE INHIBITOR
ChainResidue
AGLN1004
AGLU1094
AARG1136
AGLY1167
ALYS1168
AGLY1169
ALEU1170
ALEU1171
APRO1172
AVAL1173
ATRP1175
ALEU1181
ALYS1182
AASP1183
AGLY1184
AASN1215
AASP1232
BHOH6
B112101

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9312016
ChainResidueDetails
AASP1132

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056
ChainResidueDetails
ASER1006
ALYS1030
AGLU1077
AARG1136
AASP1150

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305
ChainResidueDetails
APHE984

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:38056462
ChainResidueDetails
ACYS1056

site_idSWS_FT_FI5
Number of Residues3
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
APTR1158
APTR1162
APTR1163

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP1132
AARG1136

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP1132
AALA1134

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP1132
AASN1137
AALA1134

site_idMCSA1
Number of Residues4
DetailsM-CSA 246
ChainResidueDetails
AASP1132increase nucleophilicity, proton acceptor, proton donor, steric role
AARG1136electrostatic stabiliser, increase electrophilicity, promote heterolysis
AASN1137metal ligand
AASP1150metal ligand

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PDB entries from 2024-07-10

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