1F21: Ribonuclease hi

Divalent metal cofactor binding in the kinetic folding trajectory of E. Coli ribonuclease hi. Determined by X-ray diffraction at 1.4 Å resolution. Released 6 Dec 2000.

Method
X-ray diffraction
Resolution
1.4 Å
Organism
Escherichia coli
Chains
1
Atoms
1,378
Mol. weight
17.53 kDa
Released
6 Dec 2000

Explore 1F21 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1F21 contains 8 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: 8 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
α-helix961
β-strand9712
α-helix981
α-helix101-11111
β-strand115-12061
α-helix128-14215
β-strand14611

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ribonuclease hiAprotein155Escherichia coliP0A7Y4 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1F21_1 RIBONUCLEASE HI (chains A)
MLKQVEIFTDGSALGNPGPGGYGAILRYRGREKTFSAGYTRTTNNRMELMAAIVALEALK
EHAEVILSTDSQYVRQGITQWIHNWKKRGWKTADKKPVKNVDLWQRLDAALGQHQIKWEW
VKGHAGHPENERADELARAAAMNPTLEDTGYQVEV

Primary citation

Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI. Goedken, E.R., Keck, J.L., Berger, J.M. et al. Protein Sci (2000) 9:1914-1921. 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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