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Crystallographic analyses of an active HIV-1 ribonuclease H domain show structural features that distinguish it from the inactive form
Analyse Crystallographic analyses of an active HIV-1 ribonuclease H domain show… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RDH
- Type
- protein
- Length
- 254 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIV-1 reverse transcriptase (ribonuclease H domain)
- EC
- 2.7.7.49
- UniProt
- P03366
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | HIV-1 reverse transcriptase (ribonuclease H domain) (EC 2.7.7.49) | protein | 127 | 0% helix, 0% strand | P03366 |
Interfaces
1 interface between chains.
- A–B · 96 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1RDH · Crystallographic analyses of an active HIV-1 ribonuclease H domain show structural… · the same entry in another collection · chain A against A, 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 P03366
- Elsewhere: RCSB PDB 1RDH · PDBe 1RDH · UniProt P03366
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