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Crystal structure of arginine kinase from the spider polybetes pythagoricus in complex with arginine

Analyse Crystal structure of arginine kinase from the spider polybetes pythagoricus in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5U92
Type
protein
Length
347 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Arginine kinase
EC
2.7.3.3
Ligands
ARG, NA
Pockets
2 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AArginine kinase (EC 2.7.3.3)protein34743% helix, 17% strand—

Ligands and binding sites

  • ARG · Arginine · ligand · chains A
  • NA · Sodium ion · metal · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11600.490.7827ARG
21080.370.7419empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

  • 5U92 · Crystal Structure of arginine kinase from the spider Polybetes pythagoricus in complex… · the same entry in another collection · chain A against A, TM-score 1.00

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