Stabilization of escherichia coli ribonuclease hi by cavity-filling mutations within a hydrophobic core. Determined by X-ray diffraction at 1.8 Å resolution. Released 31 Oct 1993.
Explore 1LAV in 3D Show helices and sheets RCSB PDB PDBe
1LAV contains 9 α-helices and 8 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 |
|---|---|---|---|
| β-strand | 5-13 | 9 | 1 |
| β-strand | 18-28 | 11 | 1 |
| β-strand | 31-42 | 12 | 1 |
| α-helix | 44-56 | 13 | |
| β-strand | 64-69 | 6 | 1 |
| α-helix | 72-76 | 5 | |
| α-helix | 77-81 | 5 | |
| α-helix | 82-87 | 6 | |
| β-strand | 91 | 1 | 2 |
| α-helix | 96 | 1 | |
| β-strand | 97 | 1 | 2 |
| α-helix | 98 | 1 | |
| α-helix | 101-111 | 11 | |
| β-strand | 115-120 | 6 | 1 |
| α-helix | 123-125 | 3 | |
| α-helix | 128-141 | 14 | |
| β-strand | 146 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ribonuclease H | A | protein | 155 | Escherichia coli | P0A7Y4 (AlphaFold model) |
>1LAV_1 RIBONUCLEASE H (chains A) MLKQVEIFTDGSCLGNPGPGGYGAILRYRGREKTFSAGYTRTTNNRMELMAAIVALEALK EHCEVILSTDSQYLRQGITQWIHNWKKRGWKTADKKPVKNVDLWQRLDAALGQHQIKWEW VKGHAGHPENERCDELARAAAMNPTLEDTGYQVEV
Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core. Ishikawa, K., Nakamura, H., Morikawa, K. et al. Biochemistry (1993) 32:6171-6178. DOI 10.1021/bi00075a009 · PubMed
Other PDB entries of the same protein (UniProt P0A7Y4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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