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1M7N

Crystal Structure of Unactivated APO Insulin-like Growth Factor-1 Receptor Kinase Domain

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 PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGvakgvvkdepetr.....VAIK
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
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 Residues16
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
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 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"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by GSK3-beta","evidences":[{"source":"UniProtKB","id":"Q60751","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q60751","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
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
AASP1132
AARG1136

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP1132
BARG1136

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP1132
AALA1134

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP1132
BALA1134

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP1132
AASN1137
AALA1134

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP1132
BASN1137
BALA1134

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PDB entries from 2025-10-08

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