Research workbench
Crystal structure of saccharomyces cerevisiae IOC4 pwwp domain fused with mbp
Analyse Crystal structure of saccharomyces cerevisiae IOC4 pwwp domain fused with mbp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E29
- Type
- protein
- Length
- 496 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,ISWI one complex protein 4
- UniProt
- P0AEX9, Q04213
- Ligands
- GLC
- Pockets
- 7 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,ISWI one complex protein 4 | protein | 496 | 41% helix, 21% strand | P0AEX9, Q04213 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 283 | 0.69 | 0.84 | 30 | GLC |
| 2 | 108 | 0.44 | 0.78 | 21 | empty |
| 3 | 61 | 0.40 | 0.80 | 20 | empty |
| 4 | 56 | 0.39 | 0.80 | 14 | empty |
| 5 | 73 | 0.37 | 0.77 | 18 | empty |
Compared structures
- 7E29 · Crystal Structure of Saccharomyces cerevisiae Ioc4 PWWP domain fused with MBP · the same entry in another collection · chain A against A, TM-score 1.00
- Q04213 · AlphaFold monomer V2.0 prediction for iswi one complex protein 4 (Q04213) · a predicted model of the same protein · chain A against A, TM-score 0.20
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 P0AEX9
- Every structure of UniProt Q04213
- Elsewhere: RCSB PDB 7E29 · PDBe 7E29 · UniProt P0AEX9 · UniProt Q04213
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