2RPI: Ribonuclease H

The NMR structure of the submillisecond folding intermediate of the Thermus thermophilus ribonuclease H. Determined by solution NMR. Released 31 Mar 2009.

Method
Solution NMR
Organism
Thermus thermophilus HB8
Chains
1
Atoms
849
Mol. weight
12.88 kDa
Released
31 Mar 2009

Explore 2RPI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2RPI contains 4 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.

Chain A: 4 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand911
β-strand1212
α-helix26-4015
β-strand4811
β-strand49-5132
α-helix57-626
α-helix66-716
β-strand7513
β-strand8113
α-helix85-9410
β-strand101-10332

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ribonuclease HAprotein112Thermus thermophilus HB8P29253 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2RPI_1 Ribonuclease H (chains A)
MNPSPRKRVALFTDGAALGNPGPGTTNNRMELKAAIEGLKALKEPAEVDLYTDSHYLKKA
FTEGWLEGWRKRGWRTAEGKPVKNRDLWEALLLAMAPHRVRFHFVKHHHHHH

Primary citation

The high-resolution NMR structure of the early folding intermediate of the Thermus thermophilus ribonuclease H. Zhou, Z., Feng, H., Ghirlando, R. et al. J Mol Biol (2008) 384:531-539. DOI 10.1016/j.jmb.2008.09.044 · PubMed

Other PDB entries of the same protein (UniProt P29253 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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