Research workbench
Cryoem structure of the pffnt-inhibitor complex
Analyse Cryoem structure of the pffnt-inhibitor complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VQR
- Type
- protein
- Length
- 1,420 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O77389
- Ligands
- R7M
Structure
electron microscopy · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 281 | — | O77389 |
| B | — | protein | 285 | — | O77389 |
| C | — | protein | 282 | — | O77389 |
| D | — | protein | 284 | — | O77389 |
| E | — | protein | 288 | — | O77389 |
Ligands and binding sites
- R7M · (2R)-2-hydroxy-7-methoxy-2-(pentafluoroethyl)-2,3-dihydro-4H-1-benzopyran-4-one · ligand · 5 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VQR · CryoEM Structure of the PfFNT-inhibitor complex · 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 O77389
- Elsewhere: RCSB PDB 6VQR · PDBe 6VQR · UniProt O77389
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