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Crystal structure of DEHYDROGENASE/ISOMERASE fabx from helicobacter pylori

Analyse Crystal structure of DEHYDROGENASE/ISOMERASE fabx from helicobacter pylori in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7E1Q
Type: protein
Length: 366 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2-nitropropane dioxygenase
UniProt: A0A0B2E3F3
Ligands: SF4, FMN, CL
Pockets: 3 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2-nitropropane dioxygenase	protein	366	40% helix, 16% strand	A0A0B2E3F3

Ligands and binding sites

SF4 · Iron/sulfur cluster · ligand · chains A
FMN · Flavin mononucleotide · ligand · chains A
CL · Chloride ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	387	0.81	0.90	60	FMN, CL
2	64	0.34	0.77	17	empty
3	50	0.25	0.73	10	empty

Compared structures

7E1Q · Crystal structure of dehydrogenase/isomerase FabX from Helicobacter pylori · the same entry in another collection · chain A against A, TM-score 1.00

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 A0A0B2E3F3
Elsewhere: RCSB PDB 7E1Q · PDBe 7E1Q · UniProt A0A0B2E3F3

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