Research workbench
Cryo-EM structure of phosphorylated ap-2 (mu E302K) bound to necap in the presence of ss DNA
Analyse Cryo-EM structure of phosphorylated ap-2 (mu E302K) bound to necap in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OXL
- Type
- protein
- Length
- 1,815 residues
- Chains
- 6
- Method
- electron microscopy
- 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
- Q9DBG3, P84091, P62744, Q9D1J1
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 6 distinct chains · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ap-2 complex subunit alpha-2 | protein | 589 | 69% helix, 1% strand | — |
| B | Ap-2 complex subunit beta | protein | 564 | 63% helix, 0% strand | Q9DBG3 |
| M | Ap-2 complex subunit mu | protein | 390 | 12% helix, 43% strand | P84091 |
| S | Ap-2 complex subunit sigma | protein | 141 | 39% helix, 23% strand | P62744 |
| N | Adaptin ear-binding coat-associated protein 2 | protein | 124 | 23% helix, 43% strand | Q9D1J1 |
| n | Unknown region of adaptin ear-binding coat-associated protein 2 ex-domain | protein | 7 | 0% helix, 0% strand | — |
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 995 | 0.85 | 0.86 | 104 | empty |
| 2 | 633 | 0.81 | 0.86 | 77 | empty |
| 3 | 789 | 0.80 | 0.83 | 65 | empty |
| 4 | 853 | 0.78 | 0.81 | 90 | empty |
| 5 | 280 | 0.73 | 0.87 | 37 | empty |
Interfaces
9 interfaces between chains.
- B–M · 3359 Ų buried · 33 hydrogen bonds · protein-protein
- A–S · 2566 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 1742 Ų buried · 22 hydrogen bonds · protein-protein
- A–M · 1067 Ų buried · 11 hydrogen bonds · protein-protein
- M–N · 789 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 6OXL · CRYO-EM STRUCTURE OF PHOSPHORYLATED AP-2 (mu E302K) BOUND TO NECAP IN THE PRESENCE OF SS… · the same entry in another collection · chain n against n, TM-score 1.00
- P62744 · AlphaFold monomer V2.0 prediction for ap-2 complex subunit sigma (P62744) · a predicted model of the same protein · chain S against A, TM-score 0.98
- Q9D1J1 · AlphaFold monomer V2.0 prediction for adaptin ear-binding coat- associated protein 2… · a predicted model of the same protein · chain N against A, TM-score 0.96
- Q9DBG3 · AlphaFold monomer V2.0 prediction for ap-2 complex subunit beta (Q9DBG3) · a predicted model of the same protein · chain B against A, TM-score 0.94
- P84091 · AlphaFold monomer V2.0 prediction for ap-2 complex subunit mu (P84091) · 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 Q9DBG3
- Every structure of UniProt P84091
- Every structure of UniProt P62744
- Every structure of UniProt Q9D1J1
- Elsewhere: RCSB PDB 6OXL · PDBe 6OXL · UniProt Q9DBG3 · UniProt P84091 · UniProt P62744 · UniProt Q9D1J1
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