Research workbench
Crystal structure of tbtudor
Analyse Crystal structure of tbtudor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IF4
- Type
- protein
- Length
- 121 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase
- EC
- 2.3.1.48
- UniProt
- D6XIY7
- Pockets
- 1 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Histone acetyltransferase (EC 2.3.1.48) | protein | 61 | 10% helix, 52% strand | D6XIY7 |
| A | Histone acetyltransferase (EC 2.3.1.48) | protein | 60 | 15% helix, 52% strand | D6XIY7 |
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 | 157 | 0.45 | 0.76 | 22 | empty |
Interfaces
1 interface between chains.
- B–A · 426 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6IF4 · Crystal structure of Tbtudor · the same entry in another collection · chain B against B, 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 D6XIY7
- Elsewhere: RCSB PDB 6IF4 · PDBe 6IF4 · UniProt D6XIY7
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