Research workbench
Three-dimensional structure of gln 25-ribonuclease T1 at 1.84 ångströms resolution: structural variations at the base recognition and catalytic sites
Analyse Three-dimensional structure of gln 25-ribonuclease T1 at 1.84 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RN1
- Type
- protein
- Length
- 310 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease T1 isozyme
- EC
- 3.1.27.3
- UniProt
- P00651
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 3 distinct chains · 16% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease T1 isozyme (EC 3.1.27.3) | protein | 103 | 17% helix, 31% strand | P00651 |
| B | Ribonuclease T1 isozyme (EC 3.1.27.3) | protein | 103 | 17% helix, 31% strand | P00651 |
| C | Ribonuclease T1 isozyme (EC 3.1.27.3) | protein | 104 | 15% helix, 31% strand | P00651 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 488 | 0.63 | 0.76 | 39 | SO4 |
| 2 | 103 | 0.49 | 0.81 | 19 | SO4 |
| 3 | 55 | 0.25 | 0.72 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–C · 356 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 213 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 131 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1RN1 · Three-dimensional structure of gln 25-ribonuclease T1 at 1.84 ångströms resolution… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P00651
- Elsewhere: RCSB PDB 1RN1 · PDBe 1RN1 · UniProt P00651
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