Research workbench
Crystal structure of ribonuclease H from thermus thermophilus HB8 refined at 2.8 ångströms resolution
Analyse Crystal structure of ribonuclease H from thermus thermophilus HB8 refined at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RIL
- Type
- protein
- Length
- 147 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease H
- EC
- 3.1.26.4
- UniProt
- P29253
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease H (EC 3.1.26.4) | protein | 147 | 38% helix, 24% strand | P29253 |
Compared structures
- 1RIL · Crystal structure of ribonuclease H from thermus thermophilus HB8 refined at 2.8… · the same entry in another collection · chain A against A, TM-score 1.00
- P29253 · AlphaFold monomer V2.0 prediction for ribonuclease H (P29253) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P29253
- Elsewhere: RCSB PDB 1RIL · PDBe 1RIL · UniProt P29253
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