Research workbench
HIV-1 reverse transcriptase Q151M:DNA binary complex
Analyse HIV-1 reverse transcriptase Q151M:DNA binary complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XN0
- Type
- protein + DNA
- Length
- 1,989 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D3XFN7
- Ligands
- GLC, FRU
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 551 | — | D3XFN7 |
| B, D | — | protein | 407 | — | D3XFN7 |
| E | — | dna | 35 | — | — |
| F | — | dna | 38 | — | — |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · chains B
- FRU · beta-D-fructofuranose · sugar · chains B
- GOL · Glycerol · additive · 5 copies · chains A, B, E, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5XN0 · HIV-1 reverse transcriptase Q151M:DNA binary complex · 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 D3XFN7
- Elsewhere: RCSB PDB 5XN0 · PDBe 5XN0 · UniProt D3XFN7
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