Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7TYR

Cryo-EM structure of the basal state of the Artemis:DNA-PKcs complex (see COMPND 13/14)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000460biological_processmaturation of 5.8S rRNA
A0000723biological_processtelomere maintenance
A0000781cellular_componentchromosome, telomeric region
A0000785cellular_componentchromatin
A0001933biological_processnegative regulation of protein phosphorylation
A0002218biological_processactivation of innate immune response
A0002376biological_processimmune system process
A0003677molecular_functionDNA binding
A0003690molecular_functiondouble-stranded DNA binding
A0003723molecular_functionRNA binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004677molecular_functionDNA-dependent protein kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005667cellular_componenttranscription regulator complex
A0005730cellular_componentnucleolus
A0005829cellular_componentcytosol
A0005958cellular_componentDNA-dependent protein kinase-DNA ligase 4 complex
A0006281biological_processDNA repair
A0006302biological_processdouble-strand break repair
A0006303biological_processdouble-strand break repair via nonhomologous end joining
A0006310biological_processDNA recombination
A0006338biological_processchromatin remodeling
A0006468biological_processprotein phosphorylation
A0006974biological_processDNA damage response
A0008630biological_processintrinsic apoptotic signaling pathway in response to DNA damage
A0016020cellular_componentmembrane
A0016233biological_processtelomere capping
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0018105biological_processpeptidyl-serine phosphorylation
A0018107biological_processpeptidyl-threonine phosphorylation
A0019899molecular_functionenzyme binding
A0019904molecular_functionprotein domain specific binding
A0031571biological_processmitotic G1 DNA damage checkpoint signaling
A0032040cellular_componentsmall-subunit processome
A0032869biological_processcellular response to insulin stimulus
A0032991cellular_componentprotein-containing complex
A0032993cellular_componentprotein-DNA complex
A0033152biological_processimmunoglobulin V(D)J recombination
A0034462biological_processsmall-subunit processome assembly
A0034511molecular_functionU3 snoRNA binding
A0035979molecular_functionhistone H2AXS139 kinase activity
A0036211biological_processprotein modification process
A0042254biological_processribosome biogenesis
A0042752biological_processregulation of circadian rhythm
A0043066biological_processnegative regulation of apoptotic process
A0045087biological_processinnate immune response
A0045621biological_processpositive regulation of lymphocyte differentiation
A0045648biological_processpositive regulation of erythrocyte differentiation
A0045727biological_processpositive regulation of translation
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0048511biological_processrhythmic process
A0048660biological_processregulation of smooth muscle cell proliferation
A0050678biological_processregulation of epithelial cell proliferation
A0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
A0070419cellular_componentnonhomologous end joining complex
A0080135biological_processregulation of cellular response to stress
A0097681biological_processdouble-strand break repair via alternative nonhomologous end joining
A0106310molecular_functionprotein serine kinase activity
A0160049biological_processnegative regulation of cGAS/STING signaling pathway
A1902036biological_processregulation of hematopoietic stem cell differentiation
A1905221biological_processpositive regulation of platelet formation
A2001034biological_processpositive regulation of double-strand break repair via nonhomologous end joining
C0000014molecular_functionsingle-stranded DNA endodeoxyribonuclease activity
C0000723biological_processtelomere maintenance
C0002250biological_processadaptive immune response
C0002376biological_processimmune system process
C0003684molecular_functiondamaged DNA binding
C0004518molecular_functionnuclease activity
C0004519molecular_functionendonuclease activity
C0004527molecular_functionexonuclease activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0006259biological_processDNA metabolic process
C0006281biological_processDNA repair
C0006303biological_processdouble-strand break repair via nonhomologous end joining
C0006310biological_processDNA recombination
C0006974biological_processDNA damage response
C0008409molecular_function5'-3' exonuclease activity
C0016787molecular_functionhydrolase activity
C0035312molecular_function5'-3' DNA exonuclease activity
C0036297biological_processinterstrand cross-link repair
C0070419cellular_componentnonhomologous end joining complex
Functional Information from PROSITE/UniProt
site_idPS00915
Number of Residues15
DetailsPI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. VKgg.EDLRQDqrveQ
ChainResidueDetails
AVAL3752-GLN3766
site_idPS00916
Number of Residues21
DetailsPI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. ShAlicIshWILgIgDRHlnN
ChainResidueDetails
ASER3907-ASN3927
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues35
DetailsRepeat: {"description":"HEAT 1"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues36
DetailsRepeat: {"description":"HEAT 2"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues33
DetailsRepeat: {"description":"TPR 1"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues633
DetailsDomain: {"description":"FAT","evidences":[{"source":"PROSITE-ProRule","id":"PRU00534","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues28
DetailsRepeat: {"description":"TPR 2"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues33
DetailsRepeat: {"description":"TPR 3"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues331
DetailsDomain: {"description":"PI3K/PI4K catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues32
DetailsDomain: {"description":"FATC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00534","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00535","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues35
DetailsRegion: {"description":"Leucine-zipper"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues22
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues6
DetailsRegion: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues8
DetailsRegion: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues25
DetailsRegion: {"description":"Activation loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsSite: {"description":"Cleavage; by caspase-3","evidences":[{"source":"PubMed","id":"8804412","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues9
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"14734805","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22977523","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34352203","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q8K4J0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8K4J0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

248942

PDB entries from 2026-02-11

PDB statisticsPDBj update infoContact PDBjnumon