Research workbench
Structure of FAM3B pander E30 construct
Analyse Structure of FAM3B pander E30 construct in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YOQ
- Type
- protein
- Length
- 542 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein FAM3B
- UniProt
- Q9D309
- Pockets
- 5 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein FAM3B | protein | 181 | 13% helix, 34% strand | Q9D309 |
| C | Protein FAM3B | protein | 180 | 13% helix, 33% strand | Q9D309 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.63 | 0.84 | 27 | empty |
| 2 | 279 | 0.62 | 0.80 | 31 | GOL |
| 3 | 56 | 0.38 | 0.80 | 14 | GOL |
| 4 | 67 | 0.28 | 0.73 | 11 | empty |
| 5 | 59 | 0.27 | 0.73 | 13 | empty |
Interfaces
2 interfaces between chains.
- A–C · 453 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 385 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
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 Q9D309
- Elsewhere: RCSB PDB 2YOQ · PDBe 2YOQ · UniProt Q9D309
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