MolNFT v1 · #187714 · protein

Structure of human KV1.3

7SSX · Potassium voltage-gated channel subfamily a member 3, green…: “Structure of human KV1.3”. Electron microscopy, 1 ligand (K), 19 pockets (best druggability 0.84). MolNFT v1 #187714 on GenesisL1: 3D structure, binding sites and…

PDB: 7SSX
Type: protein
Length: 1,384 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Potassium voltage-gated channel subfamily a member 3, green fluorescent protein fusion
UniProt: P22001
Ligands: K
Pockets: 19 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 63% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Potassium voltage-gated channel subfamily a member 3, green fluorescent protein fusion	protein	346	63% helix, 5% strand	P22001

Ligands and binding sites

K · Potassium ion · metal · 3 copies · chains A, B, C, D

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

Pockets

19 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	991	0.84	0.85	80	empty
2	909	0.80	0.82	40	empty
3	436	0.65	0.78	49	empty
4	353	0.61	0.77	29	empty
5	354	0.61	0.76	34	empty

Interfaces

6 interfaces between chains.

A–B · 2451 Å² buried · 21 hydrogen bonds · protein-protein
C–D · 2437 Å² buried · 21 hydrogen bonds · protein-protein
B–C · 2428 Å² buried · 21 hydrogen bonds · protein-protein
A–D · 2416 Å² buried · 18 hydrogen bonds · protein-protein
A–C · 12 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7SSX · Structure of human Kv1.3 · the same entry in another collection · chain D against D, TM-score 1.00
P22001 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily a member… · a predicted model of the same protein · chain D against A, TM-score 0.94

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 P22001
Elsewhere: RCSB PDB 7SSX · PDBe 7SSX · UniProt P22001

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