4J5K: Guanyl-specific ribonuclease Sa

Crystal structure analysis of Streptomyces aureofaciens ribonuclease Sa Y51F mutant. Determined by X-ray diffraction at 1.23 Å resolution. Released 28 May 2014.

Method
X-ray diffraction
Resolution
1.23 Å
Organism
Streptomyces aureofaciens
Chains
2
Atoms
2,099
Mol. weight
21.41 kDa
Released
28 May 2014

Explore 4J5K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4J5K contains 10 α-helices and 12 β-strands across 2 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.

Chain A: 6 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand5-731
α-helix8-103
α-helix13-2311
α-helix351
β-strand3611
α-helix371
α-helix45-462
β-strand52-5651
α-helix58-592
β-strand69-7351
β-strand79-8241
β-strand90-9341
Chain B: 4 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand4-742
α-helix8-103
α-helix13-2412
β-strand35-3622
α-helix371
α-helix45-462
β-strand53-5642
β-strand69-7242
β-strand79-8242
β-strand90-9342

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Guanyl-specific ribonuclease SaA, Bprotein96Streptomyces aureofaciensP05798 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4J5K_1 Guanyl-specific ribonuclease Sa (chains A, B)
DVSGTVCLSALPPEATDTLNLIASDGPFPYSQDGVVFQNRESVLPTQSYGFYHEYTVITP
GARTRGTRRIITGEATQEDYYTGDHYATFSLIDQTC

Primary citation

Contribution of hydrogen bonds to protein stability. Pace, C.N., Fu, H., Lee Fryar, K. et al. Protein Sci (2014) 23:652-661. DOI 10.1002/pro.2449 · PubMed

Other PDB entries of the same protein (UniProt P05798 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 4J5K directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.