Research workbench
Cryoem structure of apo form ZMRDR2 at 3.4 ångströms resolution
Analyse Cryoem structure of apo form ZMRDR2 at 3.4 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7W84
- Type
- protein
- Length
- 995 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-dependent RNA polymerase
- EC
- 2.7.7.48
- UniProt
- Q19VG2
- Pockets
- 15 · best druggability 0.80
Structure
electron microscopy · 1 distinct chain · 34% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA-dependent RNA polymerase (EC 2.7.7.48) | protein | 995 | 34% helix, 16% strand | Q19VG2 |
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1030 | 0.80 | 0.81 | 94 | empty |
| 2 | 475 | 0.77 | 0.85 | 67 | empty |
| 3 | 502 | 0.75 | 0.83 | 62 | empty |
| 4 | 162 | 0.68 | 0.88 | 26 | empty |
| 5 | 73 | 0.67 | 0.93 | 24 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7W84 · CryoEM structure of apo form ZmRDR2 at 3.4 Angstroms 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 7W84 · PDBe 7W84 · UniProt Q19VG2
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