Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1IR3

PHOSPHORYLATED INSULIN RECEPTOR TYROSINE KINASE IN COMPLEX WITH PEPTIDE SUBSTRATE AND ATP ANALOG

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 Residues6
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
AHOH32
AHOH52
AANP300
AMG302
AASN1137
AASP1150

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 302
ChainResidue
AHOH170
AANP300
AMG301
AASP1150
AHOH82
AHOH95
AHOH158

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ANP A 300
ChainResidue
AHOH32
AHOH52
AHOH61
AHOH74
AHOH75
AHOH76
AHOH82
AHOH103
AHOH132
AHOH158
AMG301
AMG302
ALEU1002
AGLY1005
ASER1006
AVAL1010
AALA1028
ALYS1030
AMET1076
AGLU1077
AMET1079
AASP1083
AARG1136
AASN1137
AASP1150

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
Detailsa catalytic site defined by CSA, PubMed Pichierri2003
ChainResidueDetails
AASP1132
AARG1136

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

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon