Crystal structure of human XLF/Cernunnos, a non-homologous end-joining factor. Determined by X-ray diffraction at 2.3 Å resolution. Released 11 Dec 2007.
Explore 2QM4 in 3D Show helices and sheets RCSB PDB PDBe
2QM4 contains 53 α-helices and 31 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 |
|---|---|---|---|
| α-helix | 0-9 | 10 | |
| α-helix | 12-13 | 2 | |
| β-strand | 14-17 | 4 | 1 |
| β-strand | 22-30 | 9 | 1 |
| β-strand | 33-39 | 7 | 1 |
| β-strand | 44-49 | 6 | 1 |
| α-helix | 51-61 | 11 | |
| α-helix | 69-85 | 17 | |
| β-strand | 94-100 | 7 | 1 |
| β-strand | 103-112 | 10 | 1 |
| β-strand | 115-125 | 11 | 1 |
| α-helix | 126-127 | 2 | |
| α-helix | 128-131 | 4 | |
| α-helix | 132-136 | 5 | |
| α-helix | 137-169 | 33 | |
| α-helix | 181-184 | 4 | |
| α-helix | 186-196 | 11 | |
| α-helix | 198-201 | 4 | |
| α-helix | 208-213 | 6 | |
| α-helix | 215-228 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 0-10 | 11 | |
| α-helix | 12-13 | 2 | |
| β-strand | 14-17 | 4 | 2 |
| β-strand | 22-30 | 9 | 2 |
| β-strand | 33-39 | 7 | 2 |
| β-strand | 44-49 | 6 | 2 |
| α-helix | 51-61 | 11 | |
| α-helix | 69-85 | 17 | |
| β-strand | 94-100 | 7 | 3 |
| β-strand | 103-112 | 10 | 3 |
| β-strand | 115-123 | 9 | 3 |
| β-strand | 124-125 | 2 | 2 |
| α-helix | 126-127 | 2 | |
| α-helix | 128-131 | 4 | |
| α-helix | 132-136 | 5 | |
| α-helix | 137-167 | 31 | |
| α-helix | 177-179 | 3 | |
| α-helix | 180-184 | 5 | |
| α-helix | 186-196 | 11 | |
| α-helix | 198-201 | 4 | |
| α-helix | 208-213 | 6 | |
| α-helix | 215-225 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 0-10 | 11 | |
| α-helix | 12-13 | 2 | |
| β-strand | 14-17 | 4 | 4 |
| β-strand | 22-30 | 9 | 4 |
| β-strand | 33-39 | 7 | 4 |
| β-strand | 44-50 | 7 | 4 |
| α-helix | 51-61 | 11 | |
| α-helix | 69-85 | 17 | |
| β-strand | 94-100 | 7 | 5 |
| β-strand | 103-111 | 9 | 5 |
| β-strand | 116-123 | 8 | 5 |
| β-strand | 124-125 | 2 | 4 |
| α-helix | 126-127 | 2 | |
| α-helix | 128-131 | 4 | |
| α-helix | 132-136 | 5 | |
| α-helix | 137-169 | 33 | |
| α-helix | 177-179 | 3 | |
| α-helix | 181-184 | 4 | |
| α-helix | 186-192 | 7 | |
| α-helix | 193-197 | 5 | |
| α-helix | 198-201 | 4 | |
| α-helix | 208-225 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 0-9 | 10 | |
| α-helix | 12-13 | 2 | |
| β-strand | 14-17 | 4 | 6 |
| β-strand | 22-30 | 9 | 6 |
| β-strand | 33-39 | 7 | 6 |
| β-strand | 44-50 | 7 | 6 |
| α-helix | 51-61 | 11 | |
| β-strand | 66 | 1 | 2 |
| α-helix | 69-80 | 12 | |
| β-strand | 94-100 | 7 | 6 |
| β-strand | 103-112 | 10 | 6 |
| β-strand | 115-125 | 11 | 6 |
| α-helix | 128-131 | 4 | |
| α-helix | 132-136 | 5 | |
| α-helix | 137-169 | 33 | |
| α-helix | 177-179 | 3 | |
| α-helix | 186-196 | 11 | |
| α-helix | 198-201 | 4 | |
| α-helix | 208-213 | 6 | |
| α-helix | 215-227 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Non-homologous end-joining factor 1 | A, B, C, D | protein | 235 | Homo sapiens | Q9H9Q4 (AlphaFold model) |
>2QM4_1 Non-homologous end-joining factor 1 (chains A, B, C, D) SGMEELEQGLLMQPWAWLQLAENSLLAKVFITKQGYALLVSDLQQVWHEQVDTSVVSQRA KELNKRLTAPPAAFLCHLDNLLRPLLKDAAHPSEATFSCDCVADALILRVRSELSGLPFY WNFHCMLASPSLVSQHLIRPLMGMSLALQCQVRELATLLHMKDLEIQDYQESGATLIRDR LKTEPFEENSFLEQFMIEKLPEACSIGDGKPFVMNLQDLYMAVTTQEVQVGQKHQ
Crystal structure of human XLF/Cernunnos reveals unexpected differences from XRCC4 with implications for NHEJ. Li, Y., Chirgadze, D.Y., Bolanos-Garcia, V.M. et al. EMBO J (2008) 27:290-300. DOI 10.1038/sj.emboj.7601942 · PubMed
Other PDB entries of the same protein (UniProt Q9H9Q4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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