Research workbench
Crystal structure of the second bromodomain of pleckstrin homology domain interacting protein (phip)
Analyse Crystal structure of the second bromodomain of pleckstrin homology domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MB3
- Type
- protein
- Length
- 116 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PH-interacting protein
- UniProt
- Q8WWQ0
- Ligands
- MB3
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PH-interacting protein | protein | 116 | 67% helix, 0% strand | Q8WWQ0 |
Ligands and binding sites
- MB3 · 1-methylpyrrolidin-2-one · ligand · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.51 | 0.82 | 19 | MB3 |
Compared structures
- 3MB3 · Crystal Structure of the second bromodomain of Pleckstrin homology domain interacting… · the same entry in another collection · chain A against A, 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 Q8WWQ0
- Elsewhere: RCSB PDB 3MB3 · PDBe 3MB3 · UniProt Q8WWQ0
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