Research workbench
Molecular basis for the association of pipkigamma -P90 with the clathrin adaptor ap-2
Analyse Molecular basis for the association of pipkigamma -P90 with the clathrin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3H1Z
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ap-2 complex subunit beta-1; Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma
- EC
- 2.7.1.68
- UniProt
- P62944, O60331
- Pockets
- 2 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ap-2 complex subunit beta-1 | protein | 233 | 19% helix, 41% strand | P62944 |
| P | Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma (EC 2.7.1.68) | protein | 15 | 20% helix, 13% strand | O60331 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.39 | 0.76 | 19 | empty |
| 2 | 52 | 0.32 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–P · 803 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 3H1Z · Molecular basis for the association of PIPKIgamma -p90 with the clathrin adaptor AP-2 · the same entry in another collection · chain A against A, TM-score 1.00
- P62944 · AlphaFold monomer V2.0 prediction for ap-2 complex subunit beta (P62944) · a predicted model of the same protein · chain A against A, TM-score 0.97
- O60331 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 4-phosphate 5-kinase type-1… · a predicted model of the same protein · chain P against A, TM-score 0.35
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 P62944
- Every structure of UniProt O60331
- Elsewhere: RCSB PDB 3H1Z · PDBe 3H1Z · UniProt P62944 · UniProt O60331
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