MolNFT v1 · #187536 · protein

C-type inactivation in a voltage gated K+ channel

7SIZ · Voltage-gated potassium channel subunit beta-2: “C-type inactivation in a voltage gated K+ channel”. X-ray diffraction, 2 ligands (NAP, K), 11 pockets (best druggability 0.74). MolNFT v1 #187536 on GenesisL1: 3D structure, binding…

PDB: 7SIZ
Type: protein
Length: 1,319 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Voltage-gated potassium channel subunit beta-2; Voltage gated potassium channel…
EC: 1.1.1.-
UniProt: P62483
Ligands: NAP, K
Pockets: 11 · best druggability 0.74

Structure

x-ray diffraction · 3 distinct chains · 58% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Voltage-gated potassium channel subunit beta-2 (EC 1.1.1.-)	protein	326	48% helix, 15% strand	P62483
B	Voltage gated potassium channel KV1.2-KV2.1	protein	334	64% helix, 5% strand	—
D	Voltage gated potassium channel KV1.2-KV2.1	protein	333	60% helix, 5% strand	—

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, C
K · Potassium ion · metal · 12 copies · chains B, D

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

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	349	0.74	0.86	50	NAP
2	266	0.73	0.87	45	NAP
3	254	0.56	0.77	33	empty
4	158	0.54	0.80	25	empty
5	85	0.40	0.78	19	empty

Interfaces

2 interfaces between chains.

A–B · 472 Å² buried · 5 hydrogen bonds · protein-protein
C–D · 352 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

7SIZ · C-type inactivation in a voltage gated K+ channel · the same entry in another collection · chain A against A, TM-score 1.00
P62483 · AlphaFold monomer V2.0 prediction for voltage-gated potassium channel subunit beta-2… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P62483
Elsewhere: RCSB PDB 7SIZ · PDBe 7SIZ · UniProt P62483

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