1I0V: Ribonuclease T1

Ribonuclease T1 in complex with 2'GMP (form I crystal). Determined by X-ray diffraction at 1.23 Å resolution. Released 14 Feb 2001.

Method
X-ray diffraction
Resolution
1.23 Å
Organism
Aspergillus oryzae
Chains
1
Atoms
999
Mol. weight
11.5 kDa
Ligands
2GP, CA
Released
14 Feb 2001

Explore 1I0V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1I0V contains 2 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: 2 helices, 9 β-strands

ElementResiduesLengthSheet
β-strand4-631
β-strand9-1131
α-helix13-2917
β-strand3312
β-strand3812
β-strand40-4233
β-strand56-6053
α-helix67-682
β-strand76-8163
β-strand86-9163
β-strand101-10223

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Guanyl-specific ribonuclease T1Aprotein104Aspergillus oryzaeP00651 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1I0V_1 GUANYL-SPECIFIC RIBONUCLEASE T1 (chains A)
ACDYTCGSNCYSSSDVSTAQAAGYKLHEDGETVGSNSYPHKYNNYEGFDFSVSSPYYEWP
ILSSGDVYSGGSPGADRVVFNENNQLAGVITHTGASGNNFVECT

Ligands and cofactors

IDNameFormulaCopies
2GPGuanosine-2'-monophosphateC10 H14 N5 O8 P1
CACalcium ionCa1

Primary citation

The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution. Deswarte, J., De Vos, S., Langhorst, U. et al. Eur J Biochem (2001) 268:3993-4000. DOI 10.1046/j.1432-1327.2001.02310.x · PubMed

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

Browse structure collections

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