Brct domain from DNA-repair protein XRCC1. Determined by X-ray diffraction at 3.2 Å resolution. Released 28 Feb 2000.
Explore 1CDZ in 3D Show helices and sheets RCSB PDB PDBe
1CDZ contains 4 α-helices and 5 β-strands across 1 chain. 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-13 | 4 | 1 |
| α-helix | 20-31 | 12 | |
| β-strand | 35-36 | 2 | 1 |
| β-strand | 46-48 | 3 | 1 |
| α-helix | 55-61 | 7 | |
| β-strand | 68-70 | 3 | 1 |
| α-helix | 73-79 | 7 | |
| α-helix | 87-90 | 4 | |
| β-strand | 91 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (DNA-repair protein XRCC1) | A | protein | 96 | Homo sapiens | P18887 (AlphaFold model) |
>1CDZ_1 PROTEIN (DNA-REPAIR PROTEIN XRCC1) (chains A) ELPDFFQGKHFFLYGEFPGDERRKLIRYVTAFNGELEDYMSDRVQFVITAQEWDPSFEEA LMDNPSLAFVRPRWIYSCNEKQKLLPHQLYGVVPQA
Structure of an XRCC1 BRCT domain: a new protein-protein interaction module. Zhang, X., Morera, S., Bates, P.A. et al. EMBO J (1998) 17:6404-6411. DOI 10.1093/emboj/17.21.6404 · 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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