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3D94

Crystal structure of the insulin-like growth factor-1 receptor kinase in complex with PQIP

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 Residues5
DetailsBINDING SITE FOR RESIDUE CA A 2
ChainResidue
AGLU1013
AASP1129
ATYR1131
AHOH1366
AHOH1373

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE D94 A 1
ChainResidue
AALA1001
ALYS1003
APHE1017
AMET1024
AVAL1033
AMET1049
AGLU1050
AMET1052
AASP1056
AMHO1112
AGLY1122
AASP1123
APHE1124
AHOH1354
ALEU975
AGLY976
AGLN977
APHE980

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGvakgvvkdepetr.....VAIK
ChainResidueDetails
ALEU975-LYS1003

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV
ChainResidueDetails
APHE1101-VAL1113

site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR
ChainResidueDetails
AASP1129-ARG1137

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"11694888","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18501599","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19041240","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26584640","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"11694888","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18501599","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19041240","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by GSK3-beta","evidences":[{"source":"UniProtKB","id":"Q60751","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"21994939","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP1105
AARG1109

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA1107
AASP1105

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA1107
AASP1105
AASN1110

238895

PDB entries from 2025-07-16

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