Crystal Structure of hogg1 D268E Mutant with Base-Excised DNA and 8-aminoguanine. Determined by X-ray diffraction at 1.9 Å resolution. Released 17 Feb 2004.
Explore 1M3Q in 3D Show helices and sheets RCSB PDB PDBe
1M3Q contains 19 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 | 48-51 | 4 | 1 |
| β-strand | 54-59 | 6 | 1 |
| β-strand | 62-68 | 7 | 1 |
| β-strand | 72-78 | 7 | 1 |
| α-helix | 87-89 | 3 | |
| α-helix | 90-99 | 10 | |
| α-helix | 106-116 | 11 | |
| α-helix | 118-126 | 9 | |
| α-helix | 137-147 | 11 | |
| 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 | 222-227 | 6 | |
| α-helix | 233-240 | 8 | |
| α-helix | 248-258 | 11 | |
| α-helix | 269-279 | 11 | |
| α-helix | 293-307 | 15 | |
| α-helix | 311-324 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 5'-d(*gp*gp*tp*ap*gp*ap*cp*cp*tp*gp*gp*ap*cp*gp*c)-3' | B | DNA | 15 | ||
| 5'-d(*gp*cp*gp*tp*cp*cp*ap*(drz)p*gp*tp*cp*tp*ap*cp*c)-3' | C | DNA | 15 | ||
| 8-oxoguanine DNA glycosylase | A | protein | 317 | Homo sapiens | O15527 (AlphaFold model) |
>1M3Q_1 5'-D(*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3' (chains B) GGTAGACCTGGACGC
>1M3Q_2 5'-D(*GP*CP*GP*TP*CP*CP*AP*(DRZ)P*GP*TP*CP*TP*AP*CP*C)-3' (chains C) GCGTCCANGTCTACC
>1M3Q_3 8-oxoguanine DNA glycosylase (chains A) GSEGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQ TEEQLHCTVYRGDKSQASRPTPDELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQ GVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPSLQALA GPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGT KVADCICLMALDKPQAVPVEVHMWHIAQRDYSWHPTTSQAKGPSPQTNKELGNFFRSLWG PYAGWAQAVLFSADLRQ
Structures of End Products Resulting from Lesion Processing by a DNA Glycosylase/Lyase. Chung, S.J., Verdine, G.L. Chem Biol (2004) 11:1643-1649. DOI 10.1016/j.chembiol.2004.09.014 · 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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