Research workbench
CryoEM structure of open form ZmRDR2 at 3.5 Angstroms resolution
Analyse CryoEM structure of open form ZmRDR2 at 3.5 Angstroms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7W88
- Type
- protein
- Length
- 896 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.5
- Source
- Zea mays
- Molecule
- RNA-dependent RNA polymerase
- EC
- 2.7.7.48
- UniProt
- Q19VG2
- Pockets
- 15 · best druggability 0.81
Structure
electron microscopy · resolution 3.5 · 1 distinct chain · 26% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA-dependent RNA polymerase (EC 2.7.7.48) | protein | 896 | 26% helix, 14% strand | Q19VG2 |
Pockets
15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 565 | 0.81 | 0.86 | 65 | empty |
| 2 | 212 | 0.80 | 0.93 | 45 | empty |
| 3 | 811 | 0.71 | 0.77 | 79 | empty |
| 4 | 130 | 0.63 | 0.86 | 28 | empty |
| 5 | 186 | 0.63 | 0.84 | 35 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7W88 · Cryoem structure of open form ZMRDR2 at 3.5 ångströms resolution · 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 Q19VG2
- Elsewhere: RCSB PDB 7W88 · PDBe 7W88 · UniProt Q19VG2
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