Research workbench
Structural and thermodynamic analyses of E. COLI ribonuclease hi variant with quintuple thermostabilizing mutations
Analyse Structural and thermodynamic analyses of E. COLI ribonuclease hi variant with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YV0
- Type
- protein
- Length
- 155 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease hi
- EC
- 3.1.26.4
- UniProt
- P0A7Y4
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Ribonuclease hi (EC 3.1.26.4) | protein | 155 | 36% helix, 30% strand | P0A7Y4 |
Compared structures
- 2YV0 · Structural and Thermodynamic Analyses of E. coli ribonuclease HI Variant with Quintuple… · the same entry in another collection · chain X against X, 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 P0A7Y4
- Elsewhere: RCSB PDB 2YV0 · PDBe 2YV0 · UniProt P0A7Y4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.