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Crystal structure of FAM3A
Analyse Crystal structure of FAM3A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ECQ
- Type
- protein
- Length
- 175 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein FAM3A
- UniProt
- Q9D8T0
- Ligands
- J0R, SO4
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein FAM3A | protein | 175 | 13% helix, 32% strand | Q9D8T0 |
Ligands and binding sites
- J0R · [(2R)-1-(trimethyl-$l^4-azanyl)propan-2-yl] ethanoate · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 108 | 0.41 | 0.76 | 18 | J0R |
Modifications
Observed in the structure: 2 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 Q9D8T0
- Elsewhere: RCSB PDB 7ECQ · PDBe 7ECQ · UniProt Q9D8T0
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