Research workbench
X-ray Structure of Branchiostoma floridae fluorescent protein lanFP6A
Analyse X-ray Structure of Branchiostoma floridae fluorescent protein lanFP6A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6M9Y
- Type
- protein
- Length
- 440 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.35
- Source
- Branchiostoma floridae
- Molecule
- Fluorescent protein lanFP6A
- UniProt
- C3YRA1
- Pockets
- 5 · best druggability 0.35
Structure
x-ray diffraction · resolution 1.35 · 2 distinct chains · 10% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Fluorescent protein lanFP6A | protein | 57 | 12% helix, 53% strand | C3YRA1 |
| B, D | Fluorescent protein lanFP6A | protein | 163 | 9% helix, 57% strand | C3YRA1 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 76 | 0.35 | 0.76 | 26 | empty |
| 2 | 50 | 0.34 | 0.79 | 12 | empty |
| 3 | 64 | 0.33 | 0.76 | 23 | empty |
| 4 | 63 | 0.27 | 0.73 | 15 | empty |
| 5 | 58 | 0.26 | 0.73 | 15 | empty |
Interfaces
5 interfaces between chains.
- C–D · 2357 Ų buried · 52 hydrogen bonds · protein-protein
- A–B · 2333 Ų buried · 53 hydrogen bonds · protein-protein
- B–D · 833 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 102 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 101 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6M9Y · X-ray structure of branchiostoma floridae fluorescent protein LANFP6A · 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 C3YRA1
- Elsewhere: RCSB PDB 6M9Y · PDBe 6M9Y · UniProt C3YRA1
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