Research workbench

KIRBAC3.1 mutant at a resolution of 4.1 ångströms

Analyse KIRBAC3.1 mutant at a resolution of 4.1 ångströms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6O9T
Type: protein
Length: 274 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: D9N164
Ligands: 6E3, K

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	274	—	D9N164

Ligands and binding sites

6E3 · 2,3,5,6-tetramethyl-1H,7H-pyrazolo[1,2-a]pyrazole-1,7-dione · ligand · chains A
K · Potassium ion · metal · 2 copies · chains A

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

Compared structures

6O9T · KirBac3.1 mutant at a resolution of 4.1 Angstroms · the same entry in another collection · chain A against A, TM-score 1.00
D9N164 · AlphaFold monomer V2.0 prediction for inward rectifier potassium channel KIRBAC3.1… · 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 D9N164
Elsewhere: RCSB PDB 6O9T · PDBe 6O9T · UniProt D9N164

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