MolNFT v1 · #107898 · protein
AP2 controls clathrin polymerization with a membrane-activated switch
4UQI · Ap-2 complex subunit alpha-2: “AP2 controls clathrin polymerization with a membrane-activated switch”. X-ray diffraction, 2 ligands (IHP, CL), 20 pockets (best druggability 0.85). MolNFT v1 #107898 on GenesisL1: 3D structure…
- PDB
- 4UQI
- Type
- protein
- Length
- 1,735 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ap-2 complex subunit alpha-2; Ap-2 complex subunit beta; Ap-2 complex subunit mu; Ap-2…
- UniProt
- P18484, P63010, P84092, P62743
- Ligands
- IHP, CL
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 56% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ap-2 complex subunit alpha-2 | protein | 600 | 76% helix, 1% strand | P18484 |
| B | Ap-2 complex subunit beta | protein | 597 | 68% helix, 1% strand | P63010 |
| M | Ap-2 complex subunit mu | protein | 396 | 14% helix, 46% strand | P84092 |
| S | Ap-2 complex subunit sigma | protein | 142 | 45% helix, 26% strand | P62743 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1050 | 0.85 | 0.86 | 112 | empty |
| 2 | 674 | 0.82 | 0.86 | 75 | empty |
| 3 | 793 | 0.81 | 0.84 | 92 | empty |
| 4 | 753 | 0.79 | 0.83 | 69 | empty |
| 5 | 379 | 0.73 | 0.84 | 48 | empty |
Interfaces
6 interfaces between chains.
- B–M · 3720 Ų buried · 41 hydrogen bonds · protein-protein
- A–S · 2455 Ų buried · 33 hydrogen bonds · protein-protein
- A–B · 2233 Ų buried · 33 hydrogen bonds · protein-protein
- A–M · 1222 Ų buried · 10 hydrogen bonds · protein-protein
- B–S · 649 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 4UQI · AP2 controls clathrin polymerization with a membrane-activated switch · the same entry in another collection · chain S against S, TM-score 1.00
- P62743 · AlphaFold monomer V2.0 prediction for ap-2 complex subunit sigma (P62743) · a predicted model of the same protein · chain S against A, TM-score 0.98
- P63010 · AlphaFold monomer V2.0 prediction for ap-2 complex subunit beta (P63010) · a predicted model of the same protein · chain B against A, TM-score 0.92
- P18484 · AlphaFold monomer V2.0 prediction for ap-2 complex subunit alpha-2 (P18484) · a predicted model of the same protein · chain A against A, TM-score 0.85
- P84092 · AlphaFold monomer V2.0 prediction for ap-2 complex subunit mu (P84092) · a predicted model of the same protein · chain M against A, TM-score 0.61
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 P18484
- Every structure of UniProt P63010
- Every structure of UniProt P84092
- Every structure of UniProt P62743
- Elsewhere: RCSB PDB 4UQI · PDBe 4UQI · UniProt P18484 · UniProt P63010 · UniProt P84092 · UniProt P62743
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