MolNFT v1 · #127821 · protein
Structure of the distal domain of mouse adenovirus 2 fibre, methylmercury chloride derivative
5N83 · Fiber: “Structure of the distal domain of mouse adenovirus 2 fibre, methylmercury chloride derivative”. X-ray diffraction, 1 ligand (HG), 5 pockets (best druggability 0.85). MolNFT v1 #127821 on GenesisL1: 3D structure, binding…
- PDB
- 5N83
- Type
- protein
- Length
- 585 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fiber
- UniProt
- E7CH51
- Ligands
- HG
- Pockets
- 5 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 2% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fiber | protein | 194 | 2% helix, 54% strand | E7CH51 |
| B | Fiber | protein | 195 | 2% helix, 54% strand | E7CH51 |
| C | Fiber | protein | 196 | 2% helix, 54% strand | E7CH51 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 251 | 0.85 | 0.97 | 30 | empty |
| 2 | 98 | 0.66 | 0.90 | 22 | empty |
| 3 | 302 | 0.64 | 0.80 | 35 | empty |
| 4 | 302 | 0.62 | 0.79 | 37 | empty |
| 5 | 117 | 0.45 | 0.78 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1946 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 1832 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 1821 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 5N83 · Structure of the distal domain of mouse adenovirus 2 fibre, methylmercury chloride… · 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 E7CH51
- Elsewhere: RCSB PDB 5N83 · PDBe 5N83 · UniProt E7CH51
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