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Apo human KV3.1 cryo-EM structure

Analyse Apo human KV3.1 cryo-EM structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7PQT
Type: protein
Length: 1,272 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Potassium voltage-gated channel subfamily C member 1
UniProt: P48547
Ligands: K
Pockets: 20 · best druggability 0.83

Structure

electron microscopy · 1 distinct chain · 53% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Potassium voltage-gated channel subfamily C member 1	protein	318	53% helix, 6% strand	P48547

Ligands and binding sites

K · Potassium ion · metal · 4 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	917	0.83	0.84	43	empty
2	944	0.81	0.83	64	empty
3	959	0.75	0.78	112	empty
4	615	0.66	0.75	57	empty
5	474	0.62	0.75	49	empty

Interfaces

6 interfaces between chains.

A–B · 2675 Å² buried · 14 hydrogen bonds · protein-protein
B–C · 2648 Å² buried · 16 hydrogen bonds · protein-protein
C–D · 2637 Å² buried · 16 hydrogen bonds · protein-protein
A–D · 2620 Å² buried · 12 hydrogen bonds · protein-protein
B–D · 51 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7PQT · Apo human Kv3.1 cryo-EM structure · the same entry in another collection · chain A against A, TM-score 1.00
P48547 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily C member… · a predicted model of the same protein · chain A against A, TM-score 0.92

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 P48547
Elsewhere: RCSB PDB 7PQT · PDBe 7PQT · UniProt P48547

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