Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6I83

Crystal structure of phosphorylated RET V804M tyrosine kinase domain complexed with PDD00018366

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue H72 A 1101
ChainResidue
ALEU730
AGLY810
ASER811
AARG878
ALEU881
ASER891
AASP892
APHE735
AALA756
ALYS758
AGLU775
AMET804
AGLU805
ATYR806
AALA807

site_idAC2
Number of Residues8
Detailsbinding site for residue FMT A 1102
ChainResidue
AGLY700
APRO701
ALEU702
ASER703
AGLN910
ALEU923
APHE924
AHIS926

site_idAC3
Number of Residues7
Detailsbinding site for residue FMT A 1103
ChainResidue
AARG721
ACYS794
AGLN796
AASP797
AGLY798
APRO799
ALEU801

site_idAC4
Number of Residues5
Detailsbinding site for residue FMT A 1104
ChainResidue
ATYR806
AALA807
ALYS808
AALA883
AGLU884

site_idAC5
Number of Residues5
Detailsbinding site for residue FMT A 1105
ChainResidue
ASER703
ALYS740
ATHR754
APHE924
AHOH1240

site_idAC6
Number of Residues3
Detailsbinding site for residue FMT A 1106
ChainResidue
AHIS786
ATRP856
ALYS887

site_idAC7
Number of Residues4
Detailsbinding site for residue FMT A 1107
ChainResidue
ATHR946
ALEU947
AGLY948
AGLY949

site_idAC8
Number of Residues8
Detailsbinding site for residue FMT A 1108
ChainResidue
APRO766
AGLN910
AGLY911
AMET918
ASER922
AHIS926
ATYR928
AHOH1243

site_idAC9
Number of Residues5
Detailsbinding site for residue FMT A 1109
ChainResidue
ALYS728
ALEU730
ALYS740
ATYR806
AHOH1201

site_idAD1
Number of Residues3
Detailsbinding site for residue FMT A 1110
ChainResidue
ALEU746
AARG749
ATHR753

site_idAD2
Number of Residues4
Detailsbinding site for residue FMT A 1111
ChainResidue
AARG770
ASER774
AASN777
AHOH1213

site_idAD3
Number of Residues2
Detailsbinding site for residue FMT A 1112
ChainResidue
AHIS784
AGLN860

site_idAD4
Number of Residues2
Detailsbinding site for residue FMT A 1113
ChainResidue
APHE924
AASP925

site_idAD5
Number of Residues9
Detailsbinding site for residue FMT A 1114
ChainResidue
AARG873
AASP874
ALEU875
AALA876
AARG878
AILE913
APRO914
ATRP917
ASER936

site_idAD6
Number of Residues6
Detailsbinding site for residue FMT A 1115
ChainResidue
AARG873
ALEU895
AARG897
ALYS907
AGLY911
AARG912

site_idAD7
Number of Residues5
Detailsbinding site for residue FMT A 1116
ChainResidue
AARG969
ATRP988
ALYS989
AGLN990
AHOH1239

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP874

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:24560924, ECO:0007744|PDB:4CKI
ChainResidueDetails
ALEU730

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:24560924
ChainResidueDetails
ALYS758

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:20117004, ECO:0007744|PDB:2X2M
ChainResidueDetails
AGLU805

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Cleavage; by caspase-3 => ECO:0000269|PubMed:21357690
ChainResidueDetails
AASP707

site_idSWS_FT_FI6
Number of Residues1
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

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813
ChainResidueDetails
ATYR806
ATYR809

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:24560924
ChainResidueDetails
ATYR826

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:16928683, ECO:0000269|PubMed:24560924
ChainResidueDetails
ATYR900

site_idSWS_FT_FI10
Number of Residues1
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
APTR905

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:24560924
ChainResidueDetails
ATYR981

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon