MolNFT v1 · #174917 · protein

Cryo-EM structure of the hyperpolarization-activated inwardly rectifying potassium channel KAT1 from arabidopsis

7CAL: “Cryo-EM structure of the hyperpolarization-activated inwardly rectifying potassium channel KAT1 from…”. Electron microscopy, 1 ligand (3PE), 20 pockets (best druggability 0.82). MolNFT v1 #174917 on GenesisL1: 3D structure, binding…

PDB: 7CAL
Type: protein
Length: 1,776 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Potassium channel KAT1
UniProt: Q39128
Ligands: 3PE
Pockets: 20 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 43% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Potassium channel KAT1	protein	444	43% helix, 5% strand	Q39128

Ligands and binding sites

3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · ligand · 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, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	257	0.82	0.94	41	empty
2	861	0.76	0.80	99	empty
3	870	0.76	0.79	99	empty
4	673	0.72	0.79	72	empty
5	685	0.72	0.79	75	empty

Interfaces

6 interfaces between chains.

A–B · 2690 Å² buried · 14 hydrogen bonds · protein-protein
A–D · 2689 Å² buried · 14 hydrogen bonds · protein-protein
B–C · 2687 Å² buried · 14 hydrogen bonds · protein-protein
C–D · 2684 Å² buried · 14 hydrogen bonds · protein-protein
B–D · 305 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 covalent (covalent ligand).

Compared structures

7CAL · Cryo-EM Structure of the Hyperpolarization-Activated Inwardly Rectifying Potassium… · the same entry in another collection · chain A against A, TM-score 1.00
Q39128 · AlphaFold monomer V2.0 prediction for potassium channel KAT1 (Q39128) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q39128
Elsewhere: RCSB PDB 7CAL · PDBe 7CAL · UniProt Q39128

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