Research workbench
RNase T1 mutant GLU46GLN binds the inhibitors 2'GMP and 2'AMP at the 3' subsite
Analyse RNase T1 mutant GLU46GLN binds the inhibitors 2'GMP and 2'AMP at the 3' subsite in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RGK
- Type
- protein
- Length
- 104 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease T1
- EC
- 3.1.27.3
- UniProt
- P00651
- Ligands
- 2AM, CA
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease T1 (EC 3.1.27.3) | protein | 104 | 15% helix, 31% strand | P00651 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1RGK · RNase T1 mutant GLU46GLN binds the inhibitors 2'GMP and 2'AMP at the 3' subsite · the same entry in another collection · chain A against A, TM-score 1.00
- P00651 · AlphaFold monomer V2.0 prediction for guanyl-specific ribonuclease T1 (P00651) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 1RGK · PDBe 1RGK · UniProt P00651
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