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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
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP1132
BASP1132

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU1002
BLEU1002

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS1030
BLYS1030

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000305|PubMed:7541045
ChainResidueDetails
ATYR977
BTYR977

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11694888, ECO:0000269|PubMed:18501599, ECO:0000269|PubMed:19041240
ChainResidueDetails
ATYR1158
ATYR1162
ATYR1163
BTYR1158
BTYR1162
BTYR1163

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by GSK3-beta => ECO:0000250|UniProtKB:Q60751
ChainResidueDetails
ASER1275
BSER1275

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q60751
ChainResidueDetails
ASER1279
BSER1279

site_idSWS_FT_FI8
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:21994939
ChainResidueDetails
ALYS1165
ALYS1168
BLYS1165
BLYS1168

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

226707

PDB entries from 2024-10-30

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