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Structure of a C-terminally truncated glycoside hydrolase domain from salmonella typhimurium flgj

Analyse Structure of a C-terminally truncated glycoside hydrolase domain from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5DN5
Type
protein
Length
443 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptidoglycan hydrolase flgj
EC
3.2.1.-
UniProt
P15931
Ligands
NA, IOD, CL
Pockets
5 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPeptidoglycan hydrolase flgj (EC 3.2.1.-)protein15148% helix, 15% strandP15931
CPeptidoglycan hydrolase flgj (EC 3.2.1.-)protein14146% helix, 16% strandP15931

Ligands and binding sites

  • NA · Sodium ion · metal · chains A
  • IOD · Iodide ion · ion · 10 copies · chains A, C, B
  • CL · Chloride ion · ion · 2 copies · chains C

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13030.750.8727empty
23070.680.8353NA, IOD
33230.670.8259IOD
42260.650.8344IOD
51180.440.7718empty

Interfaces

3 interfaces between chains.

  • B–C · 764 Ų buried · 12 hydrogen bonds · protein-protein
  • A–C · 721 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 689 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 5DN5 · Structure of a C-terminally truncated glycoside hydrolase domain from Salmonella… · the same entry in another collection · chain A against A, TM-score 1.00
  • P15931 · AlphaFold monomer V2.0 prediction for peptidoglycan hydrolase flgj (P15931) · a predicted model of the same protein · chain C against A, TM-score 0.93

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