1BIR: Ribonuclease T1, phe 100 to ala mutant

Ribonuclease T1, phe 100 to ala mutant complexed with 2' GMP. Determined by X-ray diffraction at 1.8 Å resolution. Released 17 Aug 1996.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Aspergillus oryzae
Chains
2
Atoms
1,747
Mol. weight
22.84 kDa
Ligands
2GP, CA
Released
17 Aug 1996

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

Secondary structure: helices and β-sheets

1BIR contains 4 α-helices and 18 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: 2 helices, 9 β-strands

ElementResiduesLengthSheet
β-strand4-631
β-strand9-1131
α-helix13-2816
β-strand3312
β-strand3812
β-strand40-4233
β-strand56-6053
α-helix66-683
β-strand76-8163
β-strand86-9163
β-strand101-10223
Chain B: 2 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand4-634
β-strand9-1134
α-helix13-2917
β-strand3315
β-strand3815
β-strand40-4236
β-strand56-6056
α-helix66-683
β-strand76-8166
β-strand86-9166
β-strand101-10226

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ribonuclease T1A, Bprotein104Aspergillus oryzaeP00651 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1BIR_1 RIBONUCLEASE T1 (chains A, B)
ACDYTCGSNCYSSSDVSTAQAAGYKLHEDGETVGSNSYPHKYNNYEGFDFSVSSPYYEWP
ILSSGDVYSGGSPGADRVVFNENNQLAGVITHTGASGNNAVECT

Ligands and cofactors

IDNameFormulaCopies
2GPGuanosine-2'-monophosphateC10 H14 N5 O8 P2
CACalcium ionCa2

Primary citation

A catalytic function for the structurally conserved residue Phe 100 of ribonuclease T1. Doumen, J., Gonciarz, M., Zegers, I. et al. Protein Sci (1996) 5:1523-1530. 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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