Research workbench
Chlamydomonas reinhardtii mastigoneme filament
Analyse Chlamydomonas reinhardtii mastigoneme filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 9B4H
- Type
- protein
- Length
- 3,925 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.1
- Source
- Chlamydomonas reinhardtii
- Molecule
- Tyrosine-protein kinase ephrin type A/B receptor-like domain-containing protein; C-type…
- UniProt
- A8J9H7, A0A2K3DRP3
- Ligands
- FUB, A1AIO, GLA, NAG, 34V
- Pockets
- 20 · best druggability 0.50
Structure
electron microscopy · resolution 3.1 · 2 distinct chains · 2% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tyrosine-protein kinase ephrin type A/B receptor-like domain-containing protein | protein | 1908 | 3% helix, 34% strand | A8J9H7 |
| X | C-type lectin domain-containing protein | protein | 109 | 0% helix, 0% strand | A0A2K3DRP3 |
Ligands and binding sites
- FUB · beta-L-arabinofuranose · sugar · 227 copies · chains A, B
- A1AIO · beta-L-glucofuranose · sugar · 114 copies · chains A, B
- GLA · alpha-D-galactopyranose · sugar · 26 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 12 copies · chains A, B
- 34V · beta-L-ribulofuranose · sugar · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.50 | 0.79 | 17 | empty |
| 2 | 215 | 0.49 | 0.75 | 38 | empty |
| 3 | 64 | 0.49 | 0.84 | 17 | empty |
| 4 | 132 | 0.48 | 0.78 | 24 | empty |
| 5 | 136 | 0.47 | 0.78 | 29 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1011 Ų buried · 9 hydrogen bonds · protein-protein
- X–B · 190 Ų buried · 0 hydrogen bonds · protein-protein
- A–X · 94 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 197 modified, 119 glycan, 54 disulfide (hydroxylation, glycosylation, disulfide, O-glycosylation, N-glycosylation).
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 A8J9H7
- Every structure of UniProt A0A2K3DRP3
- Elsewhere: RCSB PDB 9B4H · PDBe 9B4H · UniProt A8J9H7 · UniProt A0A2K3DRP3
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