Crystal Structure of Human Flap Endonuclease FEN1 (D181A) in complex with substrate 5'-flap DNA and K+. Determined by X-ray diffraction at 2.6 Å resolution. Released 27 Apr 2011.
Explore 3Q8M in 3D Show helices and sheets RCSB PDB PDBe
3Q8M contains 50 α-helices and 22 β-strands across 2 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 | 6-13 | 8 | |
| α-helix | 15-17 | 3 | |
| β-strand | 18-21 | 4 | 1 |
| α-helix | 23-26 | 4 | |
| β-strand | 30-34 | 5 | 1 |
| α-helix | 35-45 | 11 | |
| β-strand | 47 | 1 | 2 |
| β-strand | 52 | 1 | 2 |
| α-helix | 53 | 1 | |
| β-strand | 54 | 1 | 3 |
| β-strand | 60 | 1 | 3 |
| α-helix | 62-76 | 15 | |
| β-strand | 80-85 | 6 | 1 |
| α-helix | 89-90 | 2 | |
| α-helix | 91-93 | 3 | |
| α-helix | 94-115 | 22 | |
| α-helix | 120-129 | 10 | |
| α-helix | 135-148 | 14 | |
| β-strand | 152-154 | 3 | 1 |
| α-helix | 159-168 | 10 | |
| β-strand | 174-176 | 3 | 1 |
| α-helix | 181-184 | 4 | |
| β-strand | 189-192 | 4 | 1 |
| α-helix | 203 | 1 | |
| β-strand | 204-208 | 5 | 1 |
| α-helix | 209-216 | 8 | |
| α-helix | 220-231 | 12 | |
| α-helix | 243-253 | 11 | |
| α-helix | 256-262 | 7 | |
| α-helix | 269-271 | 3 | |
| α-helix | 276-284 | 9 | |
| α-helix | 295-296 | 2 | |
| α-helix | 303-306 | 4 | |
| α-helix | 307-313 | 7 | |
| α-helix | 314 | 1 | |
| α-helix | 318-333 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-13 | 8 | |
| α-helix | 15-17 | 3 | |
| β-strand | 18-21 | 4 | 4 |
| α-helix | 23-26 | 4 | |
| β-strand | 30-34 | 5 | 4 |
| α-helix | 35-45 | 11 | |
| β-strand | 47-48 | 2 | 5 |
| β-strand | 51-52 | 2 | 5 |
| α-helix | 53 | 1 | |
| β-strand | 54 | 1 | 6 |
| β-strand | 60 | 1 | 6 |
| α-helix | 62-76 | 15 | |
| β-strand | 80-85 | 6 | 4 |
| α-helix | 89-90 | 2 | |
| α-helix | 91-93 | 3 | |
| α-helix | 94-115 | 22 | |
| α-helix | 120-129 | 10 | |
| α-helix | 135-148 | 14 | |
| β-strand | 152-154 | 3 | 4 |
| α-helix | 159-168 | 10 | |
| β-strand | 174-176 | 3 | 4 |
| α-helix | 181-184 | 4 | |
| β-strand | 189-192 | 4 | 4 |
| α-helix | 203 | 1 | |
| β-strand | 204-208 | 5 | 4 |
| α-helix | 209-216 | 8 | |
| α-helix | 220-231 | 12 | |
| α-helix | 243-253 | 11 | |
| α-helix | 256-262 | 7 | |
| α-helix | 269-271 | 3 | |
| α-helix | 276-284 | 9 | |
| α-helix | 295-296 | 2 | |
| α-helix | 303-306 | 4 | |
| α-helix | 307-313 | 7 | |
| α-helix | 314 | 1 | |
| α-helix | 318-333 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Flap endonuclease 1 | A, B | protein | 341 | Homo sapiens | P39748 (AlphaFold model) |
| DNA (5'-d(*ap*cp*tp*cp*tp*gp*cp*cp*tp*cp*ap*ap*gp*ap*cp*gp*gp*t)-3') | D, G | DNA | 18 | ||
| DNA (5'-d(*tp*tp*gp*ap*gp*gp*cp*ap*gp*ap*gp*t)-3') | E, H | DNA | 12 | ||
| DNA (5'-d(*ap*cp*cp*gp*tp*cp*c)-3') | F, I | DNA | 7 |
>3Q8M_1 Flap endonuclease 1 (chains A, B) GIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETT SHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQ EVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMA CLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGI GPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEP NEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTLEVLFQ
>3Q8M_2 DNA (5'-D(*AP*CP*TP*CP*TP*GP*CP*CP*TP*CP*AP*AP*GP*AP*CP*GP*GP*T)-3') (chains D, G) ACTCTGCCTCAAGACGGT
>3Q8M_3 DNA (5'-D(*TP*TP*GP*AP*GP*GP*CP*AP*GP*AP*GP*T)-3') (chains E, H) TTGAGGCAGAGT
>3Q8M_4 DNA (5'-D(*AP*CP*CP*GP*TP*CP*C)-3') (chains F, I) ACCGTCC
Human Flap Endonuclease Structures, DNA Double-Base Flipping, and a Unified Understanding of the FEN1 Superfamily. Tsutakawa, S.E., Classen, S., Chapados, B.R. et al. Cell (2011) 145:198-211. DOI 10.1016/j.cell.2011.03.004 · PubMed
Other PDB entries of the same protein (UniProt P39748 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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