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Xpf-ERCC1 cryo-EM structure, DNA-bound form

Analyse Xpf-ERCC1 cryo-EM structure, DNA-bound form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SXB
Type
protein + DNA
Length
912 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DNA repair endonuclease xpf; DNA excision repair protein ercc-1; DNA…
EC
3.1.-.-
UniProt
Q92889, P07992
Pockets
16 · best druggability 0.78

Structure

electron microscopy · 4 distinct chains · 45% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
FDNA repair endonuclease xpf (EC 3.1.-.-)protein70147% helix, 11% strandQ92889
GDNA excision repair protein ercc-1protein19140% helix, 14% strandP07992
CDNA (5'-D(P*CP*AP*GP*AP*TP*GP*CP*TP*GP*A)-3')dna10——
DDNA (5'-D(*TP*CP*AP*GP*CP*AP*TP*CP*TP*G)-3')dna10——

Pockets

16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16210.780.8359empty
24510.770.8561empty
31260.730.9230empty
41480.610.8426empty
51400.600.8426empty

Interfaces

4 interfaces between chains.

  • F–G · 3158 Ų buried · 31 hydrogen bonds · protein-protein
  • C–D · 502 Ų buried · 30 hydrogen bonds · nucleic-nucleic
  • G–C · 283 Ų buried · 2 hydrogen bonds · protein-nucleic
  • G–D · 141 Ų buried · 0 hydrogen bonds · protein-nucleic

Compared structures

  • 6SXB · XPF-ERCC1 Cryo-EM Structure, DNA-Bound form · the same entry in another collection · chain F against F, TM-score 1.00
  • Q92889 · AlphaFold monomer V2.0 prediction for DNA repair endonuclease xpf (Q92889) · a predicted model of the same protein · chain F against A, TM-score 0.81
  • P07992 · AlphaFold monomer V2.0 prediction for DNA excision repair protein ercc-1 (P07992) · a predicted model of the same protein · chain G against A, TM-score 0.62

Analyse

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