3K77: XRCC1

X-ray crystal structure of XRCC1. Determined by X-ray diffraction at 2.6 Å resolution. Released 28 Apr 2010.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Homo sapiens
Chains
8
Atoms
9,492
Mol. weight
143.75 kDa
Released
28 Apr 2010

Explore 3K77 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3K77 contains 56 α-helices and 80 β-strands across 8 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, B, C, D, E, F, G and H: 7 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand311
α-helix4-52
β-strand6-1272
α-helix21-244
α-helix27-293
β-strand33-3421
β-strand42-54132
β-strand57-6481
β-strand67-7372
α-helix81-833
α-helix841
β-strand85-9282
α-helix96-1016
β-strand108-11141
α-helix118-1225
β-strand124-133102
β-strand143-15081

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA repair protein XRCC1A, B, C, D, E, F, G, Hprotein161Homo sapiensP18887 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>3K77_1 DNA repair protein XRCC1 (chains A, B, C, D, E, F, G, H)
MPEIRLRHVVSCSSQDSTHCAENLLKADTYRKWRAAKAGEKTISVVLQLEKEEQIHSVDI
GNDGSAFVEVLVGSSAGGAGEQDYEVLLVTSSFMSPSESRSGSNPNRVRMFGPDKLVRAA
AEKRWDRVKIVCSQPYSKDSPFGLSFVRFHSPPDKHHHHHH

Primary citation

Oxidation state of the XRCC1 N-terminal domain regulates DNA polymerase beta binding affinity. Cuneo, M.J., London, R.E. Proc Natl Acad Sci U S A (2010) 107:6805-6810. DOI 10.1073/pnas.0914077107 · PubMed

Other PDB entries of the same protein (UniProt P18887 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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