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1IRK

CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THE HUMAN INSULIN RECEPTOR

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 Residues3
DetailsBINDING SITE FOR RESIDUE EMC A 500
ChainResidue
ACYS1056
APHE1276
ASER1279

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EMC A 501
ChainResidue
AMET1109
ACYS1234

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 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
ATYR1158
ATYR1162
ATYR1163

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

218853

PDB entries from 2024-04-24

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