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4IBM

Crystal structure of insulin receptor kinase domain in complex with an inhibitor Irfin-1

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
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE IR1 A 1301
ChainResidue
ALEU1002
AMET1139
AASP1150
AMET1153
AHOH1469
AGLY1003
AVAL1010
AALA1028
AMET1076
AGLU1077
AMET1079
AALA1080
AGLY1082

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE IR1 B 1301
ChainResidue
BLEU1002
BGLY1003
BGLN1004
BALA1028
BMET1076
BGLU1077
BMET1079
BALA1080
BMET1139
BASP1150
BMET1153
BTHR1154
BILE1157

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 Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9312016
ChainResidueDetails
AASP1132
BASP1132

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056
ChainResidueDetails
ASER1006
BASP1150
ALYS1030
AGLU1077
AARG1136
AASP1150
BSER1006
BLYS1030
BGLU1077
BARG1136

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305
ChainResidueDetails
ATYR984
BTYR984

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:38056462
ChainResidueDetails
ACYS1056
BCYS1056

site_idSWS_FT_FI5
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
ATYR1158
ATYR1162
ATYR1163
BTYR1158
BTYR1162
BTYR1163

Catalytic Information from CSA
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

site_idMCSA2
Number of Residues4
DetailsM-CSA 246
ChainResidueDetails
BASP1132increase nucleophilicity, proton acceptor, proton donor, steric role
BARG1136electrostatic stabiliser, increase electrophilicity, promote heterolysis
BASN1137metal ligand
BASP1150metal ligand

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PDB entries from 2024-07-17

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