Crystal structure of product-bound human OGG1(WT). Determined by X-ray diffraction at 2.0 Å resolution. Released 15 Apr 2026.
Explore 9NZ9 in 3D Show helices and sheets RCSB PDB PDBe
9NZ9 contains 22 α-helices and 7 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 | 20-22 | 3 | |
| β-strand | 24-27 | 4 | 1 |
| α-helix | 30-32 | 3 | |
| α-helix | 35-38 | 4 | |
| β-strand | 48-51 | 4 | 1 |
| β-strand | 54-59 | 6 | 1 |
| β-strand | 62-68 | 7 | 1 |
| β-strand | 72-78 | 7 | 1 |
| α-helix | 84-85 | 2 | |
| α-helix | 87-89 | 3 | |
| α-helix | 90-99 | 10 | |
| α-helix | 106-116 | 11 | |
| α-helix | 118-124 | 7 | |
| α-helix | 137-145 | 9 | |
| α-helix | 152-166 | 15 | |
| α-helix | 168 | 1 | |
| β-strand | 169-173 | 5 | 2 |
| β-strand | 176-179 | 4 | 2 |
| α-helix | 180-183 | 4 | |
| α-helix | 184-187 | 4 | |
| α-helix | 192-198 | 7 | |
| α-helix | 204-217 | 14 | |
| α-helix | 222-226 | 5 | |
| α-helix | 227-229 | 3 | |
| α-helix | 233-240 | 8 | |
| α-helix | 248-258 | 11 | |
| α-helix | 269-279 | 11 | |
| α-helix | 293-307 | 15 | |
| α-helix | 311-323 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| N-glycosylase/DNA lyase | A | protein | 319 | Homo sapiens | O15527 (AlphaFold model) |
| DNA (5'-d(p*tp*ap*gp*ap*gp*tp*cp*(pua))-3') | C | DNA | 8 | synthetic construct | |
| DNA (5'-d(p*ap*cp*cp*tp*gp*c)-3') | B | DNA | 7 | synthetic construct | |
| DNA (5'-d(*tp*gp*cp*ap*gp*gp*tp*cp*gp*ap*cp*tp*cp*t)-3') | D | DNA | 15 | synthetic construct |
>9NZ9_1 N-glycosylase/DNA lyase (chains A) SNAGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQ TEEQLHCTVYRGDKSQASRPTPDELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQ GVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPSLQALA GPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGT KVADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGPSPQTNKELGNFFRSLWG PYAGWAQAVLFSADLRQSR
>9NZ9_2 DNA (5'-D(P*TP*AP*GP*AP*GP*TP*CP*(PUA))-3') (chains C) TAGAGTCX
>9NZ9_3 DNA (5'-D(P*AP*CP*CP*TP*GP*C)-3') (chains B) ACCTGCA
>9NZ9_4 DNA (5'-D(*TP*GP*CP*AP*GP*GP*TP*CP*GP*AP*CP*TP*CP*T)-3') (chains D) TGCAGGTCGACTCTA
A unified catalytic mechanism in bifunctional DNA glycosylases with an evolutionarily conserved aspartate-lysine dyad. Syed, A., Serafim, L.F., Arvai, A.S. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-75471-1 · PubMed
Other PDB entries of the same protein (UniProt O15527 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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