2MUT: F231L mutant ERCC1-XPF dimerization region

Solution structure of the F231L mutant ERCC1-XPF dimerization region. Determined by solution NMR. Released 24 Jun 2015.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
1,415
Mol. weight
20.22 kDa
Released
24 Jun 2015

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

Secondary structure: helices and β-sheets

2MUT contains 12 α-helices and 4 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, 3 β-strands

ElementResiduesLengthSheet
α-helix219-24022
α-helix247-25610
β-strand25911
α-helix260-2645
α-helix268-2736
α-helix279-29012
β-strand29912
β-strand30312
Chain B: 7 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix829-8313
α-helix835-8428
α-helix849-85810
α-helix862-8676
α-helix870-8778
α-helix880-89011
β-strand89311
α-helix894-8985

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA excision repair protein ERCC-1Aprotein96Homo sapiensP07992 (AlphaFold model)
DNA repair endonuclease XPFBprotein84Homo sapiensQ92889 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2MUT_1 DNA excision repair protein ERCC-1 (chains A)
RIRRRYNMADLLMEKLEQDLVSRVTECLTTVKSVNKTDSQTLLTTFGSLEQLIAASREDL
ALCPGLGPQKARRLFDVLHEPFLKVPGGLEHHHHHH
Sequence of entity 2 (B), FASTA
>2MUT_2 DNA repair endonuclease XPF (chains B)
MDSETLPESEKYNPGPQDFLLKMPGVNAKNCRSLMHHVKNIAELAALSQDELTSILGNAA
NAKQLYDFIHTSFAEVVSKGKGKK

Primary citation

The Cerebro-oculo-facio-skeletal Syndrome Point Mutation F231L in the ERCC1 DNA Repair Protein Causes Dissociation of the ERCC1-XPF Complex. Faridounnia, M., Wienk, H., Kovacic, L. et al. J Biol Chem (2015) 290:20541-20555. DOI 10.1074/jbc.M114.635169 · PubMed

Other PDB entries of the same protein (UniProt P07992 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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