Research workbench
Stabilization of escherichia COLI ribonuclease hi by cavity-filling mutations within a hydrophobic core
Analyse Stabilization of escherichia COLI ribonuclease hi by cavity-filling mutations… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LAW
- Type
- protein
- Length
- 155 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease H
- EC
- 3.1.26.4
- UniProt
- P0A7Y4
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease H (EC 3.1.26.4) | protein | 155 | 35% helix, 30% strand | P0A7Y4 |
Compared structures
- 1LAW · Stabilization of escherichia COLI ribonuclease hi by cavity-filling mutations within a… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A7Y4 · AlphaFold monomer V2.0 prediction for ribonuclease hi (P0A7Y4) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 1LAW · PDBe 1LAW · UniProt P0A7Y4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.