3QVG: XRCC1

XRCC1 bound to DNA ligase. Determined by X-ray diffraction at 2.26 Å resolution. Released 15 Jun 2011.

Method: X-ray diffraction
Resolution: 2.26 Å
Organisms: Homo sapiens, Mus musculus
Chains: 4
Atoms: 3,343
Mol. weight: 45.49 kDa
Released: 15 Jun 2011

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

Secondary structure: helices and β-sheets

3QVG contains 22 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.

Chain A: 5 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	847-848	2
β-strand	855-857	3	1
α-helix	865-874	10
β-strand	878-879	2	1
α-helix	882-887	6
β-strand	890-892	3	1
β-strand	902-904	3	1
α-helix	906-915	10
α-helix	919-921	3

Chain B: 8 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	529-531	3
α-helix	533-538	6
β-strand	545-549	5	2
α-helix	556-566	11
α-helix	569	1
β-strand	570-571	2	2
α-helix	572	1
β-strand	581-584	4	2
α-helix	590-596	7
β-strand	603-605	3	2
α-helix	607-616	10
α-helix	622-625	4
β-strand	626	1	2

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: 6 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	529-531	3
α-helix	533-536	4
β-strand	545-549	5	4
α-helix	556-566	11
β-strand	570-571	2	4
β-strand	581-584	4	4
α-helix	590-598	9
β-strand	603-605	3	4
α-helix	607-615	9
α-helix	622-625	4
β-strand	626	1	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA ligase 3	A, C	protein	89	Homo sapiens	P49916 (AlphaFold model)
DNA repair protein XRCC1	B, D	protein	106	Mus musculus	Q60596 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>3QVG_1 DNA ligase 3 (chains A, C)
SNSADETLCQTKVLLDIFTGVRLYLPPSTPDFSRLRRYFVAFDGDLVQEFDMTSATHVLG
SRDKNPAAQQVSPEWIWACIRKRRLVAPS

Sequence of entity 2 (B, D), FASTA

>3QVG_2 DNA repair protein XRCC1 (chains B, D)
MQEPPDLPVPELPDFFEGKHFFLYGEFPGDERRRLIRYVTAFNGELEDRMNERVQFVITA
QEWDPNFEEALMENPSLAFVRPRWIYSCNEKQKLLPHQLYGVVPQA

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 P49916 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3PC7 1.65 Å, X-ray crystal structure of the DNA ligase III-alpha BRCT domain.
3PC8 2.31 Å, X-ray crystal structure of the heterodimeric complex of XRCC1 and DNA ligase III-alpha…
6WH1 2.4 Å, Structure of the complex of human DNA ligase III-alpha and XRCC1 BRCT domains
10YE 2.5 Å, DNA Ligase IIIa bound to nucleosome containing a nick at SHL0
10YH 2.9 Å, DNA Ligase IIIa bound to a nucleosome containing a nick at SHL-6 (composite)
10YI 2.9 Å, XRCC1-DNA Ligase IIIa complex bound to a nucleosome containing a nick at SHL-6 (composite)
10YF 3.0 Å, DNA Ligase IIIa bound to nucleosome containing a nick at SHL-2 (composite)
3L2P 3.0 Å, Human DNA Ligase III Recognizes DNA Ends by Dynamic Switching Between Two DNA Bound States
10YG 3.4 Å, DNA Ligase IIIa bound to a nucleosome containing a nick at SHL-4 (composite)
1IMO NMR structure of human DNA ligase iiialpha brct domain
1IN1 NMR structure of human DNA ligase iiialpha brct domain
1UW0 Solution structure of the zinc-finger domain from DNA ligase IIIa

Browse structure collections

About this viewer

MolViewer shows 3QVG directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.