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UniProt P12956

X-ray repair cross-complementing protein 6 (P12956)

X-ray repair cross-complementing protein 6 (UniProt P12956), EC 3.6.4.-, 4.2.99.-: 42 experimental structures on GenesisL1, 2 ligands bound, 87 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P12956
Protein
X-ray repair cross-complementing protein 6
EC
3.6.4.-, 4.2.99.-
Experimental structures
42
Predicted models
0
Ligands
2
Pockets
87 · 14 records with a druggable one

Structures

42 records of P12956 in the MolNFT archive: 42 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1JEQCrystal Structure of the Ku Heterodimerx-ray diffractionA——
1JEQCrystal structure of the ku heterodimerx-ray diffractionA——
1JEYCrystal Structure of the Ku heterodimer bound to DNAx-ray diffractionA——
1JEYCrystal structure of the ku heterodimer bound to DNAx-ray diffractionA——
3RZXMouse importin alpha-Ku70 NLS peptide complexx-ray diffractionB——
3RZXMouse importin alpha-KU70 nls peptide complexx-ray diffractionB——
5Y3RCryo-EM structure of Human DNA-PK Holoenzymeelectron microscopyA——
5Y3RCryo-EM structure of human DNA-pk holoenzymeelectron microscopyA——
6ERFComplex of APLF factor and Ku heterodimer bound to DNAx-ray diffractionA, C, E, G——
6ERFComplex of aplf factor and ku heterodimer bound to DNAx-ray diffractionA, C, E, G——
6ERGComplex of XLF and heterodimer Ku bound to DNAx-ray diffractionA, DSO4—
6ERGComplex of xlf and heterodimer ku bound to DNAx-ray diffractionA, DSO4—
6ERHComplex of XLF and heterodimer Ku bound to DNAx-ray diffractionA, CSO4—
6ERHComplex of xlf and heterodimer ku bound to DNAx-ray diffractionA, CSO4—
6ZHACryo-EM structure of DNA-pk monomerelectron microscopyB——
6ZHECryo-EM structure of DNA-PK dimerelectron microscopyB, G—3 (best 0.89)
6ZHECryo-EM structure of DNA-pk dimerelectron microscopyB, G——
7AXZKU70/80 complex apo formelectron microscopyA——
7K0YCryo-EM structure of activated-form DNA-pk (complex VI)electron microscopyB——
7K1JCryoEM structure of inactivated-form DNA-PK (Complex III)electron microscopyB—4 (best 0.82)
7K1JCryoem structure of inactivated-form DNA-pk (complex III)electron microscopyB——
7K1KCryoem structure of inactivated-form DNA-pk (complex IV)electron microscopyB——
7K1NCryoem structure of inactivated-form DNA-pk (complex V)electron microscopyB——
7LSYNhej short-range synaptic complexelectron microscopyA, J——
7LT3NHEJ Long-range synaptic complexelectron microscopyA, J—4 (best 0.87)
7LT3Nhej long-range synaptic complexelectron microscopyA, J——
7NFCCryo-EM structure of NHEJ super-complex (dimer)electron microscopyB, G—3 (best 0.83)
7NFCCryo-EM structure of nhej super-complex (dimer)electron microscopyB, G——
7NFECryo-EM structure of NHEJ super-complex (monomer)electron microscopyB—4 (best 0.84)
7NFECryo-EM structure of nhej super-complex (monomer)electron microscopyB——
7SGLDNA-pk complex of DNA end processingelectron microscopyBIHP—
7SU3CryoEM structure of DNA-PK complex VIIelectron microscopyBIHP5 (best 0.86)
7SU3Cryoem structure of DNA-pk complex VIIelectron microscopyBIHP—
7Z6OX-Ray studies of Ku70/80 reveal the binding site for IP6x-ray diffractionAIHP13 (best 0.85)
7Z87DNA-PK in the active stateelectron microscopyB—4 (best 0.85)
7ZVTCryoEM structure of Ku heterodimer bound to DNAelectron microscopyAIHP13 (best 0.86)
7ZYGCryoEM structure of Ku heterodimer bound to DNA, PAXX and XLFelectron microscopyA—15 (best 0.87)
8BHVDNA-PK XLF mediated dimer bound to PAXXelectron microscopya, h—4 (best 0.87)
8BHYDNA-PK Ku80 mediated dimer bound to PAXX and XLFelectron microscopyB, T—2 (best 0.86)
8BOTCryo-EM structure of NHEJ supercomplex(trimer)electron microscopyG, B, T—7 (best 0.89)
8EZANHEJ Long-range complex with PAXXelectron microscopyJ, A—6 (best 0.84)
P12956AlphaFold monomer V2.0 prediction for X-ray repair cross- complementing protein 6 (P12956)———

Ligands

  • IHP · Inositol hexakisphosphate · in 5 records
  • SO4 · Sulfate ion · in 4 records

Elsewhere

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