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Chorismate mutase from bacillus subtilis at 1.30 ångström

Analyse Chorismate mutase from bacillus subtilis at 1.30 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1DBF
Type
protein
Length
381 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (chorismate mutase)
EC
5.4.99.5
UniProt
P19080
Ligands
SO4
Pockets
3 · best druggability 0.63

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CProtein (chorismate mutase) (EC 5.4.99.5)protein12731% helix, 28% strandP19080

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 9 copies · chains A, B, C
  • GOL · Glycerol · additive · 5 copies · chains A, C, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13280.630.7940SO4, GOL
23320.590.7737SO4, GOL
32550.560.7732SO4, GOL

Interfaces

3 interfaces between chains.

  • A–C · 1182 Ų buried · 14 hydrogen bonds · protein-protein
  • B–C · 1067 Ų buried · 13 hydrogen bonds · protein-protein
  • A–B · 1055 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 1DBF · Chorismate mutase from bacillus subtilis at 1.30 ångström · the same entry in another collection · chain A against A, TM-score 1.00
  • P19080 · AlphaFold monomer V2.0 prediction for chorismate mutase aroh (P19080) · a predicted model of the same protein · chain C against A, TM-score 0.92

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