MolNFT v1 · #185989 · protein
Outward-facing auxin bound form of auxin transporter PIN8
7QPA · Auxin efflux carrier component 8: “Outward-facing auxin bound form of auxin transporter PIN8”. Electron microscopy, 2 ligands (IAC, DLP), 10 pockets (best druggability 0.69). MolNFT v1 #185989 on GenesisL1: 3D structure, binding…
- PDB
- 7QPA
- Type
- protein
- Length
- 654 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Auxin efflux carrier component 8
- UniProt
- Q9LFP6
- Ligands
- IAC, DLP
- Pockets
- 10 · best druggability 0.69
Structure
electron microscopy · 1 distinct chain · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Auxin efflux carrier component 8 | protein | 327 | 77% helix, 0% strand | Q9LFP6 |
Ligands and binding sites
- IAC · 1H-indol-3-ylacetic acid · ligand · 2 copies · chains A, B
- DLP · 1,2-dilinoleoyl-sn-glycero-3-phosphocholine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.69 | 0.83 | 48 | IAC |
| 2 | 344 | 0.69 | 0.82 | 52 | IAC |
| 3 | 84 | 0.62 | 0.88 | 18 | empty |
| 4 | 113 | 0.54 | 0.82 | 19 | empty |
| 5 | 190 | 0.47 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1568 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7QPA · Outward-facing auxin bound form of auxin transporter PIN8 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9LFP6 · AlphaFold monomer V2.0 prediction for auxin efflux carrier component 8 (Q9LFP6) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9LFP6
- Elsewhere: RCSB PDB 7QPA · PDBe 7QPA · UniProt Q9LFP6
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