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7DU9

Crystal structure of human Proto-oncogene tyrosine-protein kinase receptor Ret in complex with Pralsetinib

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue Q4J A 1101
ChainResidue
AGLY731
ALEU760
ALEU772
AGLU805
ATYR806
AALA807
AGLY810
AARG878
ALEU881
AHOH1239
AHOH1266
AGLU732
AGLY733
AGLY736
ALYS737
AVAL738
AALA756
ALYS758
AMET759

site_idAC2
Number of Residues17
Detailsbinding site for residue Q4J B 1101
ChainResidue
BLEU730
BGLY731
BGLU732
BGLY733
BGLY736
BLYS737
BVAL738
BALA756
BMET759
BLEU772
BGLU805
BTYR806
BALA807
BLYS808
BGLY810
BARG878
BLEU881

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGEFGKVVkAtafhlkgragytt.....VAVK
ChainResidueDetails
ALEU730-LYS758

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHrDLAARNILV
ChainResidueDetails
ALEU870-VAL882

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
AASP874
BASP874

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:24560924, ECO:0007744|PDB:4CKI
ChainResidueDetails
ALEU730
BLEU730

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:24560924
ChainResidueDetails
ALYS758
BLYS758

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20117004, ECO:0007744|PDB:2X2M
ChainResidueDetails
AGLU805
BGLU805

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Cleavage; by caspase-3 => ECO:0000269|PubMed:21357690
ChainResidueDetails
AASP707
BASP707

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Breakpoint for translocation to form PCM1-RET; RET-CCDC6; RET-GOLGA5; RET-TRIM24 and RET-TRIM33 oncogenes => ECO:0000269|PubMed:10439047, ECO:0000269|PubMed:10980597, ECO:0000269|PubMed:2406025, ECO:0000269|PubMed:2734021
ChainResidueDetails
ALEU712
BLEU712

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813
ChainResidueDetails
ATYR806
ATYR809
BTYR806
BTYR809

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:24560924
ChainResidueDetails
ATYR826
BTYR826

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:16928683, ECO:0000269|PubMed:24560924
ChainResidueDetails
ATYR900
BTYR900

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:16928683, ECO:0000269|PubMed:20117004, ECO:0000269|PubMed:24560924, ECO:0000269|PubMed:28846099
ChainResidueDetails
ATYR905
BTYR905

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:24560924
ChainResidueDetails
ATYR981
BTYR981

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PDB entries from 2024-07-24

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