Research workbench
The NMR structure of the submillisecond folding intermediate of the thermus thermophilus ribonuclease H
Analyse The NMR structure of the submillisecond folding intermediate of the thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RPI
- Type
- protein
- Length
- 106 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease H
- EC
- 3.1.26.4
- UniProt
- P29253
Structure
solution nmr · 1 distinct chain · 35% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease H (EC 3.1.26.4) | protein | 106 | 35% helix, 10% strand | P29253 |
Compared structures
- 2RPI · The NMR structure of the submillisecond folding intermediate of the Thermus thermophilus… · 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 0.80
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 2RPI · PDBe 2RPI · UniProt P29253
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