2A1J: DNA repair endonuclease XPF

Crystal Structure of the Complex between the C-Terminal Domains of Human XPF and ERCC1. Determined by X-ray diffraction at 2.7 Å resolution. Released 2 Aug 2005.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Homo sapiens
Chains
2
Atoms
1,094
Mol. weight
17.37 kDa
Ligands
HG
Released
2 Aug 2005

Explore 2A1J in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2A1J 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-helix839-8424
α-helix849-85810
α-helix862-8665
α-helix870-8778
α-helix880-89112
Chain B: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix221-23919
α-helix247-25711
α-helix260-2645
α-helix268-2725
α-helix280-29011

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA repair endonuclease XPFAprotein63Homo sapiensQ92889 (AlphaFold model)
DNA excision repair protein ERCC-1Bprotein91Homo sapiensP07992 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2A1J_1 DNA repair endonuclease XPF (chains A)
MPQDFLLKMPGVNAKNCRSLMHHVKNIAELAALSQDELTSILGNAANAKQLYDFIHTSFA
EVV
Sequence of entity 2 (B), FASTA
>2A1J_2 DNA excision repair protein ERCC-1 (chains B)
MGSSHHHHHHSQDPADLLMEKLEQDFVSRVTECLTTVKSVNKTDSQTLLTTFGSLEQLIA
ASREDLALCPGLGPQKARRLFDVLHEPFLKV

Ligands and cofactors

IDNameFormulaCopies
HGMercury (II) ionHg1

Primary citation

Crystal structure and DNA binding functions of ERCC1, a subunit of the DNA structure-specific endonuclease XPF-ERCC1. Tsodikov, O.V., Enzlin, J.H., Scharer, O.D. et al. Proc Natl Acad Sci U S A (2005) 102:11236-11241. DOI 10.1073/pnas.0504341102 · 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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