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Udp-manganese complex of spsa from bacillus subtilis

Analyse Udp-manganese complex of spsa 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
1QGQ
Type
protein
Length
238 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (spore coat polysaccharide biosynthesis protein spsa)
UniProt
P39621
Ligands
UDP, MN, MG
Pockets
1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (spore coat polysaccharide biosynthesis protein spsa)protein23838% helix, 27% strandP39621

Ligands and binding sites

  • UDP · Uridine-5'-diphosphate · ligand · chains A
  • MN · Manganese (II) ion · metal · chains A
  • MG · Magnesium ion · metal · chains A
  • GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13090.560.7635MN, MG, UDP, GOL

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1QGQ · Udp-manganese complex of spsa from bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00
  • P39621 · AlphaFold monomer V2.0 prediction for spore coat polysaccharide biosynthesis protein spsa… · a predicted model of the same protein · chain A against A, TM-score 0.98

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