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.
Explore 1BIR in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 1 |
| β-strand | 9-11 | 3 | 1 |
| α-helix | 13-28 | 16 | |
| β-strand | 33 | 1 | 2 |
| β-strand | 38 | 1 | 2 |
| β-strand | 40-42 | 3 | 3 |
| β-strand | 56-60 | 5 | 3 |
| α-helix | 66-68 | 3 | |
| β-strand | 76-81 | 6 | 3 |
| β-strand | 86-91 | 6 | 3 |
| β-strand | 101-102 | 2 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 4 |
| β-strand | 9-11 | 3 | 4 |
| α-helix | 13-29 | 17 | |
| β-strand | 33 | 1 | 5 |
| β-strand | 38 | 1 | 5 |
| β-strand | 40-42 | 3 | 6 |
| β-strand | 56-60 | 5 | 6 |
| α-helix | 66-68 | 3 | |
| β-strand | 76-81 | 6 | 6 |
| β-strand | 86-91 | 6 | 6 |
| β-strand | 101-102 | 2 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ribonuclease T1 | A, B | protein | 104 | Aspergillus oryzae | P00651 (AlphaFold model) |
>1BIR_1 RIBONUCLEASE T1 (chains A, B) ACDYTCGSNCYSSSDVSTAQAAGYKLHEDGETVGSNSYPHKYNNYEGFDFSVSSPYYEWP ILSSGDVYSGGSPGADRVVFNENNQLAGVITHTGASGNNAVECT
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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