MolNFT v1 · #8993 · protein + DNA
RNA dependent RNA polymerase from dsrna bacteriophage PHI6 plus template
1HHT · DNA (5'-(*TP*TP*TP*CP*C)-3'): “RNA dependent RNA polymerase from dsrna bacteriophage PHI6 plus template”. X-ray diffraction, 1 ligand (MN), 11 pockets (best druggability 0.84). MolNFT v1 #8993 on GenesisL1: 3D structure, binding…
- PDB
- 1HHT
- Type
- protein + DNA
- Length
- 2,007 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (5'-(*TP*TP*TP*CP*C)-3'); P2 protein
- UniProt
- P11124
- Ligands
- MN
- Pockets
- 11 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, E, F | DNA (5'-(*TP*TP*TP*CP*C)-3') | dna | 5 | — | — |
| P, Q, R | P2 protein | protein | 664 | 45% helix, 15% strand | P11124 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 3 copies · chains P, Q, R
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 939 | 0.84 | 0.86 | 93 | empty |
| 2 | 943 | 0.84 | 0.85 | 90 | empty |
| 3 | 974 | 0.84 | 0.85 | 99 | empty |
| 4 | 1084 | 0.81 | 0.82 | 70 | empty |
| 5 | 551 | 0.76 | 0.84 | 52 | empty |
Interfaces
6 interfaces between chains.
- E–Q · 969 Ų buried · 15 hydrogen bonds · protein-nucleic
- F–R · 968 Ų buried · 15 hydrogen bonds · protein-nucleic
- D–P · 966 Ų buried · 15 hydrogen bonds · protein-nucleic
- P–Q · 962 Ų buried · 15 hydrogen bonds · protein-protein
- P–R · 503 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1HHT · RNA dependent RNA polymerase from dsRNA bacteriophage phi6 plus template · the same entry in another collection · chain D against D, 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 P11124
- Elsewhere: RCSB PDB 1HHT · PDBe 1HHT · UniProt P11124
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