Research workbench
Structure of P51G cyanovirin-N swapped dimer in the P21212 space group
Analyse Structure of P51G cyanovirin-N swapped dimer in the P21212 space group in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4J4D
- Type
- protein
- Length
- 404 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyanovirin-N
- UniProt
- P81180
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, B | Cyanovirin-N | protein | 101 | 13% helix, 58% strand | P81180 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 871 | 0.74 | 0.78 | 94 | empty |
| 2 | 59 | 0.31 | 0.76 | 14 | empty |
Interfaces
6 interfaces between chains.
- C–D · 3421 Ų buried · 70 hydrogen bonds · protein-protein
- A–B · 3404 Ų buried · 62 hydrogen bonds · protein-protein
- A–C · 346 Ų buried · 8 hydrogen bonds · protein-protein
- D–B · 280 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 267 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 8 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 4J4D · PDBe 4J4D · UniProt P81180
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