MolNFT v2 · #155529 · protein + DNA
HIV-1 reverse transcriptase with Q151M/Y115F/F116Y:DNA:dCTP ternary complex
6KDK: “HIV-1 reverse transcriptase with Q151M/Y115F/F116Y:DNA:dCTP ternary complex”. X-ray diffraction at 2.56, 4 ligands (DCP, GLC, FRU). MolNFT v2 #155529 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6KDK
- Type
- protein + DNA
- Length
- 1,991 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.56
- Source
- Human immunodeficiency virus 1; Human immunodeficiency virus type 1; SYNTHETIC…
- UniProt
- D3XFN5, P12497
- Ligands
- DCP, GLC, FRU, MG
Structure
x-ray diffraction · resolution 2.56 · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 553 | — | D3XFN5 |
| B, D | — | protein | 406 | — | P12497 |
| E | — | dna | 35 | — | — |
| F | — | dna | 38 | — | — |
Ligands and binding sites
- DCP · 2'-deoxycytidine-5'-triphosphate · ligand · 2 copies · chains A, E, C, F
- GLC · alpha-D-glucopyranose · sugar · chains B
- FRU · beta-D-fructofuranose · sugar · chains B, E
- MG · Magnesium ion · metal · 2 copies · chains A, C
- GOL · Glycerol · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6KDK · HIV-1 reverse transcriptase with Q151M/Y115F/F116Y:DNA:DCTP ternary 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 D3XFN5
- Every structure of UniProt P12497
- Elsewhere: RCSB PDB 6KDK · PDBe 6KDK · UniProt D3XFN5 · UniProt P12497
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.