Crystal Structure of R192F hFen1 in complex with DNA. Determined by X-ray diffraction at 2.3 Å resolution. Released 30 Jan 2019.
Explore 5ZOG in 3D Show helices and sheets RCSB PDB PDBe
5ZOG contains 24 α-helices and 11 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 |
|---|---|---|---|
| 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 | 47-48 | 2 | 2 |
| β-strand | 51-52 | 2 | 2 |
| 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 | 91-99 | 9 | |
| α-helix | 129-131 | 3 | |
| 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 | 194-200 | 7 | |
| α-helix | 203 | 1 | |
| β-strand | 204-208 | 5 | 1 |
| α-helix | 209-216 | 8 | |
| α-helix | 220-230 | 11 | |
| α-helix | 243-253 | 11 | |
| α-helix | 256-262 | 7 | |
| α-helix | 269-271 | 3 | |
| α-helix | 276-284 | 9 | |
| α-helix | 291-293 | 3 | |
| α-helix | 299-301 | 3 | |
| α-helix | 303-306 | 4 | |
| α-helix | 307-313 | 7 | |
| α-helix | 318-339 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Flap endonuclease 1 | A | protein | 344 | Homo sapiens | P39748 (AlphaFold model) |
| DNA (5'-d(*cp*cp*cp*gp*tp*cp*c)-3') | B | DNA | 7 | synthetic construct | |
| DNA (5'-d(p*tp*cp*cp*tp*cp*tp*gp*cp*cp*tp*cp*ap*ap*gp*ap*cp*gp*gp*g)-3') | C | DNA | 19 | synthetic construct | |
| DNA (5'-d(*tp*gp*ap*gp*gp*cp*ap*gp*ap*gp*gp*ap*t)-3') | D | DNA | 13 | synthetic construct |
>5ZOG_1 Flap endonuclease 1 (chains A) MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGET TSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAE QEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDM DCLTFGSPVLMFHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRG IGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSE PNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQKLAAALEHHHH
>5ZOG_2 DNA (5'-D(*CP*CP*CP*GP*TP*CP*C)-3') (chains B) CCCGTCC
>5ZOG_3 DNA (5'-D(P*TP*CP*CP*TP*CP*TP*GP*CP*CP*TP*CP*AP*AP*GP*AP*CP*GP*GP*G)-3') (chains C) TCCTCTGCCTCAAGACGGG
>5ZOG_4 DNA (5'-D(*TP*GP*AP*GP*GP*CP*AP*GP*AP*GP*GP*AP*T)-3') (chains D) TGAGGCAGAGGAT
Structural basis of 5' flap recognition and protein-protein interactions of human flap endonuclease 1. Xu, H., Shi, R., Han, W. et al. Nucleic Acids Res (2018) 46:11315-11325. DOI 10.1093/nar/gky911 · 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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