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Crystal structure of N-terminal G-domain of enga from bacillus subtilis

Analyse Crystal structure of N-terminal G-domain of enga from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5X4B
Type
protein
Length
296 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
GTPase der
UniProt
P50743
Ligands
GDP, K, MG, NA
Pockets
2 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGTPase derprotein15239% helix, 24% strandP50743
BGTPase derprotein14440% helix, 23% strandP50743

Ligands and binding sites

  • GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
  • K · Potassium ion · metal · 3 copies · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains A, B
  • NA · Sodium ion · metal · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11540.540.8029K
2600.260.7222NA

Interfaces

1 interface between chains.

  • A–B · 643 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 5X4B · Crystal Structure of N-terminal G-domain of EngA from Bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00
  • P50743 · AlphaFold monomer V2.0 prediction for GTPase der (P50743) · a predicted model of the same protein · chain B against A, TM-score 0.99

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