Research workbench
Structure of viperin from trichoderma virens
Analyse Structure of viperin from trichoderma virens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B4C
- Type
- protein
- Length
- 3,107 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- G9MQB8
- Ligands
- SO4
Structure
x-ray diffraction · 12 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 259 | — | G9MQB8 |
| B | — | protein | 260 | — | G9MQB8 |
| C | — | protein | 260 | — | G9MQB8 |
| D | — | protein | 261 | — | G9MQB8 |
| E | — | protein | 256 | — | G9MQB8 |
| F | — | protein | 260 | — | G9MQB8 |
| G | — | protein | 259 | — | G9MQB8 |
| H | — | protein | 259 | — | G9MQB8 |
| I | — | protein | 257 | — | G9MQB8 |
| J | — | protein | 258 | — | G9MQB8 |
| K | — | protein | 260 | — | G9MQB8 |
| L | — | protein | 258 | — | G9MQB8 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 24 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
- FLC · Citrate anion · additive · 12 copies · chains A, G, B, J, C, D, K, E, H, F, L, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6B4C · Structure of Viperin from Trichoderma virens · 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 G9MQB8
- Elsewhere: RCSB PDB 6B4C · PDBe 6B4C · UniProt G9MQB8
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