MolNFT v1 · #177972 · protein

Cryoem structure of human KV4.2

7F0J · Potassium voltage-gated channel subfamily D member 2: “Cryoem structure of human KV4.2”. Electron microscopy, 1 ligand (ZN), 20 pockets (best druggability 0.82). MolNFT v1 #177972 on GenesisL1: 3D structure, binding sites and…

PDB: 7F0J
Type: protein
Length: 1,544 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Potassium voltage-gated channel subfamily D member 2
UniProt: Q9NZV8
Ligands: ZN
Pockets: 20 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 67% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, C, F, H	Potassium voltage-gated channel subfamily D member 2	protein	386	67% helix, 3% strand	Q9NZV8

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains B, H, C, F

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	541	0.82	0.88	42	empty
2	946	0.80	0.82	51	empty
3	771	0.72	0.77	80	empty
4	723	0.71	0.77	80	empty
5	592	0.69	0.78	68	empty

Interfaces

6 interfaces between chains.

B–H · 2743 Å² buried · 21 hydrogen bonds · protein-protein
B–C · 2742 Å² buried · 21 hydrogen bonds · protein-protein
F–H · 2738 Å² buried · 21 hydrogen bonds · protein-protein
C–F · 2734 Å² buried · 21 hydrogen bonds · protein-protein
B–F · 53 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7F0J · CryoEM structure of human Kv4.2 · the same entry in another collection · chain B against B, TM-score 1.00
Q9NZV8 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily D member… · a predicted model of the same protein · chain B against A, TM-score 0.82

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 Q9NZV8
Elsewhere: RCSB PDB 7F0J · PDBe 7F0J · UniProt Q9NZV8

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