Research workbench
Structure of P51G cyanovirin-N swapped tetramer in the P212121 space group
Analyse Structure of P51G cyanovirin-N swapped tetramer in the P212121 space group in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4J4F
- 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
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, C, B, A | Cyanovirin-N | protein | 101 | 11% helix, 59% strand | P81180 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 641 | 0.66 | 0.76 | 65 | empty |
| 2 | 187 | 0.52 | 0.78 | 29 | empty |
| 3 | 59 | 0.28 | 0.74 | 13 | empty |
Interfaces
5 interfaces between chains.
- D–C · 2461 Ų buried · 46 hydrogen bonds · protein-protein
- B–A · 2402 Ų buried · 38 hydrogen bonds · protein-protein
- C–B · 1518 Ų buried · 36 hydrogen bonds · protein-protein
- C–A · 1385 Ų buried · 29 hydrogen bonds · protein-protein
- D–B · 1383 Ų buried · 25 hydrogen bonds · 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 4J4F · PDBe 4J4F · UniProt P81180
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