Research workbench
Pandda analysis group deposition of models with modelled events (E.G. bound ligands) -- crystal structure of human FAM83B in complex with FMOPL000010A
Analyse Pandda analysis group deposition of models with modelled events (E.G. bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5QHO
- Type
- protein
- Length
- 164 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein FAM83B
- UniProt
- Q5T0W9
- Ligands
- GOY
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein FAM83B | protein | 164 | 35% helix, 30% strand | Q5T0W9 |
Ligands and binding sites
- GOY · di(piperidin-1-yl)methanone · ligand · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5QHO · PanDDA analysis group deposition of models with modelled events (e.g. bound ligands)… · the same entry in another collection · chain A against A, TM-score 1.00
- Q5T0W9 · AlphaFold monomer V2.0 prediction for protein FAM83B (Q5T0W9) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q5T0W9
- Elsewhere: RCSB PDB 5QHO · PDBe 5QHO · UniProt Q5T0W9
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