MolNFT v1 · #50278 · protein
Five site mutated cyanovirin-N with mannose dimer bound
2RDK: “Five site mutated cyanovirin-N with mannose dimer bound”. X-ray diffraction, 1 ligand (MAN), 2 pockets (best druggability 0.37). MolNFT v1 #50278 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2RDK
- Type
- protein
- Length
- 200 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyanovirin-N
- UniProt
- P81180
- Ligands
- MAN
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyanovirin-N | protein | 101 | 13% helix, 57% strand | P81180 |
| B | Cyanovirin-N | protein | 99 | 13% helix, 57% strand | P81180 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.37 | 0.77 | 14 | empty |
| 2 | 120 | 0.36 | 0.73 | 19 | MAN |
Interfaces
1 interface between chains.
- A–B · 445 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
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 P81180
- Elsewhere: RCSB PDB 2RDK · PDBe 2RDK · UniProt P81180
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.