MolNFT v1 · #143509 · protein + DNA
Hydrogen bonding complementary, not size complementarity is key in the formation of the double helix
6B1R · Reverse transcriptase: “Hydrogen bonding complementary, not size complementarity is key in the formation of the double helix”. X-ray diffraction, 2 pockets (best druggability 0.50). MolNFT v1 #143509 on GenesisL1: 3D structure…
- PDB
- 6B1R
- Type
- protein + DNA
- Length
- 258 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Reverse transcriptase; DNA (5'-D(*CP*TP*TP*AP*TP*(1WA)P*(1WA)P*(1WA))-3'); DNA…
- EC
- 2.7.7.49
- UniProt
- P03355
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 3 distinct chains · 32% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Reverse transcriptase (EC 2.7.7.49) | protein | 242 | 32% helix, 22% strand | P03355 |
| B | DNA (5'-D(*CP*TP*TP*AP*TP*(1WA)P*(1WA)P*(1WA))-3') | dna | 8 | — | — |
| G | DNA (5'-D(P*(IGU)P*(IGU)P*(IGU)P*AP*TP*AP*AP*G)-3') | dna | 8 | — | — |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.50 | 0.78 | 30 | empty |
| 2 | 60 | 0.27 | 0.73 | 10 | empty |
Interfaces
3 interfaces between chains.
- B–G · 349 Ų buried · 33 hydrogen bonds · nucleic-nucleic
- A–B · 249 Ų buried · 4 hydrogen bonds · protein-nucleic
- A–G · 200 Ų buried · 3 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 6 modified (nucleotide modification).
Compared structures
- 6B1R · Hydrogen Bonding Complementary, not size complementarity is key in the formation of the… · 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 P03355
- Elsewhere: RCSB PDB 6B1R · PDBe 6B1R · UniProt P03355
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