Mycobacterium tuberculosis dUTPase complexed with magnesium and dUDP. Determined by X-ray diffraction at 3.0 Å resolution. Released 16 Mar 2004.
Explore 1SLH in 3D Show helices and sheets RCSB PDB PDBe
1SLH contains 13 α-helices and 36 β-strands across 3 chains. 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 |
|---|---|---|---|
| β-strand | 4-9 | 6 | 1 |
| α-helix | 15-17 | 3 | |
| β-strand | 27-30 | 4 | 2 |
| α-helix | 31 | 1 | |
| β-strand | 35-37 | 3 | 3 |
| β-strand | 42-46 | 5 | 4 |
| β-strand | 49-52 | 4 | 1 |
| α-helix | 53-54 | 2 | |
| β-strand | 57-62 | 6 | 2 |
| α-helix | 65-70 | 6 | |
| β-strand | 73-75 | 3 | 4 |
| β-strand | 80-83 | 4 | 2 |
| β-strand | 91-96 | 6 | 4 |
| β-strand | 103-105 | 3 | 3 |
| β-strand | 110-118 | 9 | 2 |
| β-strand | 123-127 | 5 | 5 |
| α-helix | 130-133 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-9 | 6 | 6 |
| α-helix | 15-17 | 3 | |
| β-strand | 26-30 | 5 | 7 |
| α-helix | 31 | 1 | |
| β-strand | 35-37 | 3 | 8 |
| β-strand | 42-46 | 5 | 9 |
| β-strand | 49-52 | 4 | 6 |
| α-helix | 53-54 | 2 | |
| β-strand | 57-63 | 7 | 7 |
| α-helix | 65-70 | 6 | |
| β-strand | 73-75 | 3 | 9 |
| α-helix | 78 | 1 | |
| β-strand | 80-83 | 4 | 7 |
| β-strand | 91-96 | 6 | 9 |
| β-strand | 103-105 | 3 | 8 |
| β-strand | 110-118 | 9 | 7 |
| β-strand | 123-126 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-9 | 6 | 5 |
| α-helix | 15-17 | 3 | |
| β-strand | 26-30 | 5 | 10 |
| β-strand | 35-37 | 3 | 11 |
| β-strand | 42-46 | 5 | 12 |
| β-strand | 49-52 | 4 | 5 |
| α-helix | 53-54 | 2 | |
| β-strand | 57-62 | 6 | 10 |
| α-helix | 65-71 | 7 | |
| β-strand | 73-75 | 3 | 12 |
| β-strand | 80-82 | 3 | 10 |
| β-strand | 91-96 | 6 | 12 |
| β-strand | 103-105 | 3 | 11 |
| β-strand | 110-118 | 9 | 10 |
| β-strand | 123-126 | 4 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Deoxyuridine 5'-triphosphate nucleotidohydrolase | A, B, C | protein | 174 | Mycobacterium tuberculosis | P9WNS5 (AlphaFold model) |
>1SLH_1 Deoxyuridine 5'-triphosphate nucleotidohydrolase (chains A, B, C) MGSSHHHHHHSSGLVPRGSHMSTTLAIVRLDPGLPLPSRAHDGDAGVDLYSAEDVELAPG RRALVRTGVAVAVPFGMVGLVHPRSGLATRVGLSIVNSPGTIDAGYRGEIKVALINLDPA APIVVHRGDRIAQLLVQRVELVELVEVSSFDEAGLASTSRGDGGHGSSGGHASL
Water and common crystallization additives (TRS) are not listed.
Crystal structure of the Mycobacterium tuberculosis dUTPase: insights into the catalytic mechanism. Chan, S., Segelke, B., Lekin, T. et al. J Mol Biol (2004) 341:503-517. DOI 10.1016/j.jmb.2004.06.028 · PubMed
Other PDB entries of the same protein (UniProt P9WNS5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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