Research workbench
Cryoem structure of human KV4.2-DPP6S complex, extracellular region
Analyse Cryoem structure of human KV4.2-DPP6S complex, extracellular region in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E89
- Type
- protein
- Length
- 2,916 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dipeptidyl aminopeptidase-like protein 6
- UniProt
- P42658
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 1 distinct chain · 14% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| J, I, A, B | Dipeptidyl aminopeptidase-like protein 6 | protein | 729 | 14% helix, 29% strand | P42658 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 875 | 0.80 | 0.82 | 88 | empty |
| 2 | 789 | 0.79 | 0.82 | 103 | empty |
| 3 | 1061 | 0.76 | 0.78 | 104 | empty |
| 4 | 500 | 0.70 | 0.80 | 48 | empty |
| 5 | 95 | 0.68 | 0.92 | 28 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1834 Ų buried · 17 hydrogen bonds · protein-protein
- J–I · 1834 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide (disulfide).
Compared structures
- 7E89 · CryoEM structure of human Kv4.2-DPP6S complex, extracellular region · the same entry in another collection · chain B against B, TM-score 1.00
- P42658 · AlphaFold monomer V2.0 prediction for dipeptidyl aminopeptidase-like protein 6 (P42658) · a predicted model of the same protein · chain I against A, TM-score 0.98
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 P42658
- Elsewhere: RCSB PDB 7E89 · PDBe 7E89 · UniProt P42658
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