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Structure of the glycoside hydrolase domain from salmonella typhimurium flgj

Analyse Structure of the glycoside hydrolase domain from salmonella typhimurium flgj in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DN4
Type: protein
Length: 159 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidoglycan hydrolase flgj
EC: 3.2.1.-
UniProt: P15931
Ligands: IOD, CL
Pockets: 1 · best druggability 0.27

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidoglycan hydrolase flgj (EC 3.2.1.-)	protein	159	58% helix, 9% strand	P15931

Ligands and binding sites

IOD · Iodide ion · ion · 11 copies · chains A
CL · Chloride ion · ion · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	57	0.27	0.72	9	empty

Compared structures

5DN4 · Structure of the glycoside hydrolase domain from Salmonella typhimurium FlgJ · 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 A against A, TM-score 0.96

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P15931
Elsewhere: RCSB PDB 5DN4 · PDBe 5DN4 · UniProt P15931

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