Research workbench
Structural study of mutants of escherichia COLI ribonuclease hi with enhanced thermostability
Analyse Structural study of mutants of escherichia COLI ribonuclease hi with enhanced… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RBV
- 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 · 37% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease H (EC 3.1.26.4) | protein | 155 | 37% helix, 30% strand | P0A7Y4 |
Compared structures
- 1RBV · Structural study of mutants of escherichia COLI ribonuclease hi with enhanced… · 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 1RBV · PDBe 1RBV · UniProt P0A7Y4
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