Research workbench
Crystal structure of WIPI2 in complex with W2IR of ATG16L1
Analyse Crystal structure of WIPI2 in complex with W2IR of ATG16L1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MU2
- Type
- protein
- Length
- 658 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Wd repeat domain phosphoinositide-interacting protein 2; Autophagy-related protein 16-1
- UniProt
- E7EVC7
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 4% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Wd repeat domain phosphoinositide-interacting protein 2 | protein | 309 | 0% helix, 55% strand | — |
| B | Autophagy-related protein 16-1 | protein | 21 | 81% helix, 0% strand | E7EVC7 |
| C | Wd repeat domain phosphoinositide-interacting protein 2 | protein | 316 | 0% helix, 54% strand | — |
| D | Autophagy-related protein 16-1 | protein | 12 | 58% helix, 0% strand | E7EVC7 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 730 | 0.79 | 0.83 | 66 | empty |
| 2 | 1182 | 0.78 | 0.80 | 89 | empty |
| 3 | 74 | 0.36 | 0.77 | 15 | empty |
Interfaces
4 interfaces between chains.
- A–B · 624 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 580 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 334 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 73 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 7MU2 · Crystal Structure of WIPI2 in complex with W2IR of ATG16L1 · 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 E7EVC7
- Elsewhere: RCSB PDB 7MU2 · PDBe 7MU2 · UniProt E7EVC7
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