1DET: Ribonuclease T1 carboxymethylated at glu 58

Ribonuclease T1 carboxymethylated at glu 58 in complex with 2'GMP. Determined by X-ray diffraction at 1.8 Å resolution. Released 11 Jul 1996.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Aspergillus oryzae
Chains
1
Atoms
892
Mol. weight
11.56 kDa
Ligands
2GP
Released
11 Jul 1996

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

Secondary structure: helices and β-sheets

1DET contains 5 α-helices and 11 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: 5 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand4-631
β-strand9-1131
α-helix13-2917
β-strand3312
β-strand3812
β-strand40-4233
α-helix531
α-helix551
β-strand56-6053
β-strand6114
α-helix661
β-strand6714
α-helix681
β-strand76-8163
β-strand86-9163
β-strand101-10223

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ribonuclease T1Aprotein104Aspergillus oryzaeP00651 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1DET_1 RIBONUCLEASE T1 (chains A)
ACDYTCGSNCYSSSDVSTAQAAGYQLHEDGETVGSNSYPHKYNNYEGFDFSVSSPYYEWP
ILSSGDVYSGGSPGADRVVFNENNQLAGVITHTGASGNNFVECT

Ligands and cofactors

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

Water and common crystallization additives (NA) are not listed.

Primary citation

Crystal structure of ribonuclease T1 carboxymethylated at Glu58 in complex with 2'-GMP. Ishikawa, K., Suzuki, E., Tanokura, M. et al. Biochemistry (1996) 35:8329-8334. DOI 10.1021/bi960493d · 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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