MolNFT v1 · #184325 · protein
BETA2 appendage domain of AP2 bound to terminal domains beneath the hub of the 28 triskelia mini clathrin coat complex, class 15
7OM8 · Clathrin heavy chain: “BETA2 appendage domain of AP2 bound to terminal domains beneath the hub of the 28 triskelia mini clathrin…”. Electron microscopy, 6 pockets (best druggability 0.67). MolNFT v1 #184325 on GenesisL1: 3D…
- PDB
- 7OM8
- Type
- protein
- Length
- 539 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Clathrin heavy chain; Ap-2 complex subunit beta
- UniProt
- I3LGD4, P63010
- Pockets
- 6 · best druggability 0.67
Structure
electron microscopy · 3 distinct chains · 9% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| Y | Clathrin heavy chain | protein | 157 | 2% helix, 47% strand | I3LGD4 |
| Z | Clathrin heavy chain | protein | 149 | 2% helix, 48% strand | I3LGD4 |
| B | Ap-2 complex subunit beta | protein | 233 | 18% helix, 41% strand | P63010 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 511 | 0.67 | 0.78 | 41 | empty |
| 2 | 427 | 0.61 | 0.76 | 48 | empty |
| 3 | 180 | 0.45 | 0.74 | 30 | empty |
| 4 | 85 | 0.36 | 0.75 | 18 | empty |
| 5 | 60 | 0.35 | 0.78 | 18 | empty |
Interfaces
2 interfaces between chains.
- Y–B · 540 Ų buried · 3 hydrogen bonds · protein-protein
- Z–B · 380 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 7OM8 · Beta2 appendage domain of AP2 bound to terminal domains beneath the hub of the 28… · the same entry in another collection · chain Y against Y, TM-score 1.00
- 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 0.99
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 I3LGD4
- Every structure of UniProt P63010
- Elsewhere: RCSB PDB 7OM8 · PDBe 7OM8 · UniProt I3LGD4 · UniProt P63010
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