MolNFT v1 · #152819 · protein
Cryo-EM structure of the plant actin filaments from zea mays pollen
6IUG · Pollen F-actin: “Cryo-EM structure of the plant actin filaments from zea mays pollen”. Electron microscopy, 2 ligands (ADP, MG), 18 pockets (best druggability 0.83). MolNFT v1 #152819 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6IUG
- Type
- protein
- Length
- 1,855 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pollen F-actin
- UniProt
- B6TQ08
- Ligands
- ADP, MG
- Pockets
- 18 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Pollen F-actin | protein | 371 | 36% helix, 18% strand | B6TQ08 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains A, B, C, D, E
- MG · Magnesium ion · metal · 5 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1013 | 0.83 | 0.84 | 122 | empty |
| 2 | 257 | 0.79 | 0.92 | 50 | ADP, MG |
| 3 | 262 | 0.79 | 0.91 | 49 | ADP, MG |
| 4 | 282 | 0.78 | 0.90 | 52 | ADP, MG |
| 5 | 293 | 0.78 | 0.90 | 50 | ADP, MG |
Interfaces
7 interfaces between chains.
- A–C · 1119 Ų buried · 13 hydrogen bonds · protein-protein
- C–E · 1111 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 1110 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 535 Ų buried · 5 hydrogen bonds · protein-protein
- D–E · 532 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 6IUG · Cryo-EM structure of the plant actin filaments from Zea mays pollen · 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 B6TQ08
- Elsewhere: RCSB PDB 6IUG · PDBe 6IUG · UniProt B6TQ08
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