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Crystal structure of arginine kinase (AK3) from the ciliate paramecium tetraurelia

Analyse Crystal structure of arginine kinase (AK3) from the ciliate paramecium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7EWS
Type
protein
Length
756 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Arginine kinase
UniProt
A0C7I4
Pockets
8 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BArginine kinaseprotein37841% helix, 17% strandA0C7I4

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16850.740.8055empty
22520.690.8532empty
34470.690.8138empty
42890.640.8125empty
51420.530.8032empty

Interfaces

1 interface between chains.

  • A–B · 1028 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 7EWS · Crystal structure of arginine kinase (AK3) from the ciliate Paramecium tetraurelia · the same entry in another collection · chain A against A, TM-score 1.00

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