1RN4: Ribonuclease T1

HIS92ALA mutation in ribonuclease T1 induces segmental flexibility. An X-ray study. Determined by X-ray diffraction at 1.8 Å resolution. Released 15 Jan 1993.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Aspergillus oryzae
Chains
1
Atoms
845
Mol. weight
11.12 kDa
Ligands
PO4
Released
15 Jan 1993

Explore 1RN4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1RN4 contains 4 α-helices and 9 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, 9 β-strands

ElementResiduesLengthSheet
β-strand4-631
β-strand9-1131
α-helix13-2917
β-strand3312
β-strand3812
β-strand40-4233
α-helix531
α-helix551
β-strand56-6163
α-helix66-683
β-strand76-8163
β-strand86-9273
β-strand100-10233

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ribonuclease T1Aprotein104Aspergillus oryzaeP00651 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1RN4_1 RIBONUCLEASE T1 (chains A)
ACDYTCGSNCYSSSDVSTAQAAGYKLHEDGETVGSNSYPHKYNNYEGFDFSVSSPYYEWP
ILSSGDVYSGGSPGADRVVFNENNQLAGVITATGASGNNFVECT

Ligands and cofactors

IDNameFormulaCopies
PO4Phosphate ionO4 P1

Primary citation

His92Ala mutation in ribonuclease T1 induces segmental flexibility. An X-ray study. Koellner, G., Choe, H.W., Heinemann, U. et al. J Mol Biol (1992) 224:701-713. DOI 10.1016/0022-2836(92)90554-W · PubMed

Other PDB entries of the same protein (UniProt P00651 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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