Fidelity properties and structure of M282L mutator mutant of DNA polymerase: subtle structural changes influence the mechanism of nucleotide discrimination. Determined by X-ray diffraction at 2.35 Å resolution. Released 3 Aug 2001.
Explore 1JN3 in 3D Show helices and sheets RCSB PDB PDBe
1JN3 contains 16 α-helices and 9 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 | 92-100 | 9 | |
| α-helix | 108-116 | 9 | |
| α-helix | 122-126 | 5 | |
| α-helix | 129-131 | 3 | |
| α-helix | 134-141 | 8 | |
| α-helix | 145-147 | 3 | |
| β-strand | 150-151 | 2 | 1 |
| α-helix | 152-169 | 18 | |
| β-strand | 174-177 | 4 | 2 |
| α-helix | 179-182 | 4 | |
| β-strand | 187-188 | 2 | 1 |
| β-strand | 191-196 | 6 | 2 |
| α-helix | 208-220 | 13 | |
| β-strand | 224-230 | 7 | 2 |
| β-strand | 234-239 | 6 | 2 |
| α-helix | 250-252 | 3 | |
| β-strand | 253-259 | 7 | 2 |
| α-helix | 262-264 | 3 | |
| α-helix | 265-271 | 7 | |
| α-helix | 276-288 | 13 | |
| β-strand | 291-293 | 3 | 3 |
| β-strand | 298-300 | 3 | 3 |
| α-helix | 310-312 | 3 | |
| α-helix | 316-322 | 7 | |
| α-helix | 330-332 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA polymerase beta | A | protein | 251 | Rattus norvegicus | P06766 (AlphaFold model) |
>1JN3_1 DNA POLYMERASE BETA (chains A) LEKIRQDDTSSSINFLTRVTGIGPSAARKLVDEGIKTLEDLRKNEDKLNHHQRIGLKYFE DFEKRIPREEMLQMQDIVLNEVKKLDPEYIATVCGSFRRGAESSGDMDVLLTHPNFTSES SKQPKLLHRVVEQLQKVRFITDTLSKGETKFMGVCQLPSENDENEYPHRRIDIRLIPKDQ YYCGVLYFTGSDIFNKNLRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEQDIFDYIQ WRYREPKDRSE
A DNA polymerase beta mutator mutant with reduced nucleotide discrimination and increased protein stability. Shah, A.M., Conn, D.A., Li, S.-X. et al. Biochemistry (2001) 40:11372-11381. DOI 10.1021/bi010755y · PubMed
Other PDB entries of the same protein (UniProt P06766 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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