Native Structure of the Human 8-oxoguanine DNA Glycosylase hOGG1. Determined by X-ray diffraction at 2.15 Å resolution. Released 9 Jan 2002.
Explore 1KO9 in 3D Show helices and sheets RCSB PDB PDBe
1KO9 contains 20 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 | 35-38 | 4 | |
| β-strand | 47-51 | 5 | 1 |
| β-strand | 54-58 | 5 | 1 |
| β-strand | 63-68 | 6 | 1 |
| β-strand | 72-77 | 6 | 1 |
| α-helix | 87-89 | 3 | |
| α-helix | 90-99 | 10 | |
| α-helix | 106-116 | 11 | |
| α-helix | 118-126 | 9 | |
| 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 | 181-183 | 3 | |
| α-helix | 184-188 | 5 | |
| α-helix | 192-199 | 8 | |
| α-helix | 205-213 | 9 | |
| α-helix | 214-218 | 5 | |
| α-helix | 222-228 | 7 | |
| α-helix | 233-240 | 8 | |
| α-helix | 248-257 | 10 | |
| α-helix | 269-279 | 11 | |
| α-helix | 293-307 | 15 | |
| α-helix | 311-322 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 8-oxoguanine DNA glycosylase | A | protein | 345 | Homo sapiens | O15527 (AlphaFold model) |
>1KO9_1 8-oxoguanine DNA glycosylase (chains A) MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLA DQVWTLTQTEEQLHCTVYRGDKSQASRPTPDELEAVRKYFQLDVTLAQLYHHWGSVDSHF QEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHG FPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKAL CILPGVGTKVADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGPSPQTNKELG NFFRSLWGPYAGWAQAVLFSADLRQSRHAQEPPAKRRKGSKGPEG
Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase. Bjoras, M., Seeberg, E., Luna, L. et al. J Mol Biol (2002) 317:171-177. DOI 10.1006/jmbi.2002.5400 · 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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