3PC8: DNA repair protein XRCC1

X-ray crystal structure of the heterodimeric complex of XRCC1 and DNA ligase III-alpha BRCT domains. Determined by X-ray diffraction at 2.31 Å resolution. Released 15 Jun 2011.

Method: X-ray diffraction
Resolution: 2.31 Å
Organisms: Mus musculus, Homo sapiens
Chains: 4
Atoms: 3,137
Mol. weight: 43.56 kDa
Ligands: MG
Released: 15 Jun 2011

Explore 3PC8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3PC8 contains 16 α-helices and 18 β-strands across 4 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.

Chains A and B: 5 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	545-549	5	1
α-helix	556-566	11
β-strand	570-571	2	1
β-strand	581-584	4	1
α-helix	587-588	2
α-helix	590-598	9
β-strand	603-605	3	1
α-helix	607-616	10
α-helix	622-625	4
β-strand	626	1	1

Chain C: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	855-857	3	3
α-helix	865-874	10
β-strand	878-879	2	3
α-helix	882-887	6
β-strand	890-892	3	3
β-strand	902-904	3	3
α-helix	906-915	10

Chain D: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	855-857	3	4
α-helix	865-874	10
β-strand	878-879	2	4
α-helix	885-887	3
β-strand	890-892	3	4
β-strand	902-904	3	4
α-helix	906-915	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA repair protein XRCC1	A, B	protein	98	Mus musculus	Q60596 (AlphaFold model)
DNA ligase 3	C, D	protein	88	Homo sapiens	P49916 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3PC8_1 DNA repair protein XRCC1 (chains A, B)
MPELPDFFEGKHFFLYGEFPGDERRRLIRYVTAFNGELEDRMNERVQFVITAQEWDPNFE
EALMENPSLAFVRPRWIYSCNEKQKLLPHQLYGVVPQA

Sequence of entity 2 (C, D), FASTA

>3PC8_2 DNA ligase 3 (chains C, D)
GSADETLSQTKVLLDIFTGVRLYLPPSTPDFSRLRRYFVAFDGDLVQEFDMTSATHVLGS
RDKNPAAQQVSPEWIWACIRKRRLVAPS

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1

Water and common crystallization additives (TRS) are not listed.

Primary citation

The structural basis for partitioning of the XRCC1/DNA ligase III-{alpha} BRCT-mediated dimer complexes. Cuneo, M.J., Gabel, S.A., Krahn, J.M. et al. Nucleic Acids Res (2011) 39:7816-7827. DOI 10.1093/nar/gkr419 · PubMed

Other PDB entries of the same protein (UniProt Q60596 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3PC6 1.9 Å, X-ray crystal structure of the second XRCC1 BRCT domain.
3QVG 2.26 Å, XRCC1 bound to DNA ligase

Browse structure collections

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