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Crystal structure of NA,K-ATPase N-domain

Analyse Crystal structure of NA,K-ATPase N-domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Q3I
Type
protein
Length
192 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
NA,K-ATPase
EC
3.6.3.9
Ligands
NI
Pockets
1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANA,K-ATPase (EC 3.6.3.9)protein19228% helix, 31% strand—

Ligands and binding sites

  • NI · Nickel (II) ion · metal · 3 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11770.500.7726empty

Compared structures

  • 1Q3I · Crystal Structure of Na,K-ATPase N-domain · the same entry in another collection · chain A against A, TM-score 1.00

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