Research workbench
Crystal structure of the middle double pH domain of human fact complex subunit SPT16
Analyse Crystal structure of the middle double pH domain of human fact complex subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UMU
- Type
- protein
- Length
- 516 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fact complex subunit SPT16
- UniProt
- Q9Y5B9
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fact complex subunit SPT16 | protein | 258 | 25% helix, 39% strand | Q9Y5B9 |
| B | Fact complex subunit SPT16 | protein | 258 | 26% helix, 39% strand | Q9Y5B9 |
Ligands and binding sites
- FMT · Formic acid · additive · 25 copies · chains A, B
- ACT · Acetate ion · additive · 5 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 873 | 0.74 | 0.78 | 83 | FMT |
| 2 | 121 | 0.40 | 0.75 | 19 | FMT |
| 3 | 75 | 0.30 | 0.73 | 19 | FMT |
Interfaces
1 interface between chains.
- A–B · 554 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 5UMU · Crystal structure of the middle double PH domain of human FACT complex subunit SPT16 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y5B9 · AlphaFold monomer V2.0 prediction for fact complex subunit SPT16 (Q9Y5B9) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q9Y5B9
- Elsewhere: RCSB PDB 5UMU · PDBe 5UMU · UniProt Q9Y5B9
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