X-ray crystal structure of reduced XRCC1 bound to DNA pol beta catalytic domain. Determined by X-ray diffraction at 2.95 Å resolution. Released 28 Apr 2010.
Explore 3K75 in 3D Show helices and sheets RCSB PDB PDBe
3K75 contains 39 α-helices and 48 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 1 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-12 | 7 | 2 |
| α-helix | 21-24 | 4 | |
| β-strand | 33-34 | 2 | 1 |
| β-strand | 38 | 1 | 3 |
| β-strand | 40 | 1 | 3 |
| β-strand | 42-54 | 13 | 2 |
| β-strand | 57-64 | 8 | 1 |
| β-strand | 67-73 | 7 | 2 |
| β-strand | 85-92 | 8 | 2 |
| α-helix | 96-100 | 5 | |
| β-strand | 108-111 | 4 | 1 |
| α-helix | 113-115 | 3 | |
| α-helix | 118-122 | 5 | |
| β-strand | 124-133 | 10 | 2 |
| β-strand | 143-150 | 8 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 4 |
| β-strand | 8-12 | 5 | 5 |
| β-strand | 33-34 | 2 | 6 |
| β-strand | 42-48 | 7 | 5 |
| β-strand | 53 | 1 | 7 |
| β-strand | 58-62 | 5 | 6 |
| β-strand | 67-73 | 7 | 5 |
| β-strand | 85-92 | 8 | 5 |
| α-helix | 96-101 | 6 | |
| β-strand | 108-111 | 4 | 6 |
| α-helix | 113-115 | 3 | |
| β-strand | 116 | 1 | 5 |
| β-strand | 125 | 1 | 7 |
| β-strand | 127-133 | 7 | 5 |
| β-strand | 143-149 | 7 | 6 |
| β-strand | 150 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 93-100 | 8 | |
| α-helix | 108-116 | 9 | |
| α-helix | 122-125 | 4 | |
| α-helix | 129-131 | 3 | |
| α-helix | 134-141 | 8 | |
| α-helix | 143-147 | 5 | |
| β-strand | 150-151 | 2 | 8 |
| α-helix | 152-169 | 18 | |
| β-strand | 174-177 | 4 | 9 |
| α-helix | 179-182 | 4 | |
| β-strand | 187-188 | 2 | 8 |
| β-strand | 191-196 | 6 | 9 |
| α-helix | 208-220 | 13 | |
| β-strand | 224-230 | 7 | 9 |
| β-strand | 234-239 | 6 | 9 |
| α-helix | 248-252 | 5 | |
| β-strand | 253-259 | 7 | 9 |
| α-helix | 262-264 | 3 | |
| α-helix | 265-273 | 9 | |
| α-helix | 276-288 | 13 | |
| β-strand | 291-293 | 3 | 10 |
| β-strand | 298-300 | 3 | 10 |
| β-strand | 301 | 1 | 11 |
| β-strand | 307 | 1 | 11 |
| α-helix | 309-312 | 4 | |
| α-helix | 316-323 | 8 | |
| α-helix | 326-329 | 4 | |
| α-helix | 330-332 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 94-101 | 8 | |
| α-helix | 108-116 | 9 | |
| α-helix | 122-127 | 6 | |
| α-helix | 129-131 | 3 | |
| α-helix | 134-141 | 8 | |
| β-strand | 150-151 | 2 | 12 |
| α-helix | 152-169 | 18 | |
| β-strand | 174-177 | 4 | 13 |
| α-helix | 180-183 | 4 | |
| β-strand | 187-188 | 2 | 12 |
| β-strand | 191-196 | 6 | 13 |
| α-helix | 208-220 | 13 | |
| β-strand | 224-230 | 7 | 13 |
| β-strand | 234-240 | 7 | 13 |
| α-helix | 249-251 | 3 | |
| β-strand | 252-259 | 8 | 13 |
| α-helix | 262-264 | 3 | |
| α-helix | 265-273 | 9 | |
| α-helix | 276-288 | 13 | |
| β-strand | 291-294 | 4 | 14 |
| β-strand | 297-300 | 4 | 14 |
| β-strand | 301 | 1 | 15 |
| β-strand | 307 | 1 | 15 |
| α-helix | 309-312 | 4 | |
| α-helix | 316-322 | 7 | |
| α-helix | 330-332 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA repair protein XRCC1 | B, C | protein | 189 | Homo sapiens | P18887 (AlphaFold model) |
| DNA polymerase beta | D, E | protein | 252 | Rattus norvegicus | P06766 (AlphaFold model) |
>3K75_1 DNA repair protein XRCC1 (chains B, C) MPEIRLRHVVSCSSQDSTHCAENLLKADTYRKWRAAKAGEKTISVVLQLEKEEQIHSVDI GNDGSAFVEVLVGSSAGGAGEQDYEVLLVTSSFMSPSESRSGSNPNRVRMFGPDKLVRAA AEKRWDRVKIVCSQPYSKDSPFGLSFVRFHSPPDKDEAEAPSQKVTVTKLGQFRVKEEDE SANHHHHHH
>3K75_2 DNA polymerase beta (chains D, E) MDDTSSSINFLTRVTGIGPSAARKLVDEGIKTLEDLRKNEDKLNHHQRIGLKYFEDFEKR IPREEMLQMQDIVLNEVKKLDPEYIATVCGSFRRGAESSGDMDVLLTHPNFTSESSKQPK LLHRVVEQLQKVRFITDTLSKGETKFMGVCQLPSENDENEYPHRRIDIRLIPKDQYYCGV LYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEQDIFDYIQWRYRE PKDRSEHHHHHH
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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