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6NEC

STRUCTURE OF RET PROTEIN TYROSINE KINASE DOMAIN IN COMPLEX WITH NINTEDANIB

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue XIN A 1101
ChainResidue
AGLY731
AALA807
ALYS808
AGLY810
ALEU881
AASP892
AALA756
ALYS758
AGLU775
ALEU779
AILE788
AVAL804
AGLU805
ATYR806

site_idAC2
Number of Residues6
Detailsbinding site for residue FMT A 1102
ChainResidue
AARG873
ALEU895
AARG897
ALYS907
AGLY911
AARG912

site_idAC3
Number of Residues8
Detailsbinding site for residue FMT C 1101
ChainResidue
AGLN910
ALEU923
APHE924
AHIS926
CGLY700
CPRO701
CLEU702
CSER703

site_idAC4
Number of Residues19
Detailsbinding site for residue XIN C 1102
ChainResidue
CTHR729
CLEU730
CGLY731
CVAL738
CALA756
CLYS758
CGLU775
CLEU779
CILE788
CVAL804
CGLU805
CTYR806
CALA807
CLYS808
CTYR809
CGLY810
CLEU881
CSER891
CASP892

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
CASP874

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:24560924, ECO:0007744|PDB:4CKI
ChainResidueDetails
ALEU730
CLEU730

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:24560924
ChainResidueDetails
ALYS758
CLYS758

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20117004, ECO:0007744|PDB:2X2M
ChainResidueDetails
AGLU805
CGLU805

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Cleavage; by caspase-3 => ECO:0000269|PubMed:21357690
ChainResidueDetails
AASP707
CASP707

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
CLEU712

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813
ChainResidueDetails
ATYR806
ATYR809
CTYR806
CTYR809

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:24560924
ChainResidueDetails
ATYR826
CTYR826

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
CTYR900

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
CTYR905

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:24560924
ChainResidueDetails
ATYR981
CTYR981

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PDB entries from 2024-11-06

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