MolNFT v1 · #101688 · protein
The emcv 3DPOL structure at 2.8A resolution
4NZ0 · Genome polyprotein: “The emcv 3DPOL structure at 2.8A resolution”. X-ray diffraction, 1 ligand (CL), 20 pockets (best druggability 0.73). MolNFT v1 #101688 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4NZ0
- Type
- protein
- Length
- 2,760 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Genome polyprotein
- EC
- 2.7.7.48
- UniProt
- P12296
- Ligands
- CL
- Pockets
- 20 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Genome polyprotein (EC 2.7.7.48) | protein | 460 | 42% helix, 17% strand | P12296 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 804 | 0.73 | 0.78 | 74 | empty |
| 2 | 573 | 0.73 | 0.81 | 54 | empty |
| 3 | 880 | 0.72 | 0.77 | 77 | empty |
| 4 | 655 | 0.72 | 0.79 | 76 | empty |
| 5 | 810 | 0.71 | 0.77 | 74 | empty |
Interfaces
8 interfaces between chains.
- D–F · 1085 Ų buried · 11 hydrogen bonds · protein-protein
- A–E · 635 Ų buried · 12 hydrogen bonds · protein-protein
- B–E · 621 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 443 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 443 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 4NZ0 · The EMCV 3Dpol structure at 2.8A 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 P12296
- Elsewhere: RCSB PDB 4NZ0 · PDBe 4NZ0 · UniProt P12296
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