2AQ0: Human homodimeric dna repair protein XPF

Solution structure of the human homodimeric dna repair protein XPF. Determined by solution NMR. Released 3 Oct 2006.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
1,292
Mol. weight
18.46 kDa
Released
3 Oct 2006

Explore 2AQ0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2AQ0 contains 10 α-helices and 0 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 5 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix16-216
α-helix28-3710
α-helix41-466
α-helix49-568
α-helix59-7012
Chain B: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix114-1218
α-helix128-13710
α-helix141-1466
α-helix149-1568
α-helix159-16911

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA repair endonuclease XPFA, Bprotein84Homo sapiensQ92889 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2AQ0_1 DNA repair endonuclease XPF (chains A, B)
MDSETLPESEKYNPGPQDFLLKMPGVNAKNCRSLMHHVKNIAELAALSQDELTSILGNAA
NAKQLYDFIHTSFAEVVSKGKGKK

Primary citation

The HhH domain of the human DNA repair protein XPF forms stable homodimers. Das, D., Tripsianes, K., Jaspers, N.G. et al. Proteins (2008) 70:1551-1563. DOI 10.1002/prot.21635 · PubMed

Other PDB entries of the same protein (UniProt Q92889 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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