1LAW: Ribonuclease H

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.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Escherichia coli
Chains
1
Atoms
1,350
Mol. weight
17.64 kDa
Released
31 Oct 1993

Explore 1LAW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1LAW contains 7 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.

Chain A: 7 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand5-1391
β-strand18-28111
β-strand31-42121
α-helix44-5714
β-strand64-6961
α-helix72-765
α-helix77-815
α-helix82-876
β-strand9112
β-strand9712
α-helix981
α-helix101-11111
β-strand115-12061
α-helix128-14114
β-strand14611

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ribonuclease HAprotein155Escherichia coliP0A7Y4 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1LAW_1 RIBONUCLEASE H (chains A)
MLKQVEIFTDGSCLGNPGPGGYGAILRYRGREKTFSAGYTRTTNNRMELMAAIVALEALK
EHCEVILSTDSQYIRQGITQWIHNWKKRGWKTADKKPVKNVDLWQRLDAALGQHQIKWEW
VKGHAGHPENERCDELARAAAMNPTLEDTGYQVEV

Primary citation

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:

Browse structure collections

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