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Crystal structure of dihydroorotate dehydrogenase from schistosoma mansoni

Analyse Crystal structure of dihydroorotate dehydrogenase from schistosoma mansoni in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UY4
Type: protein
Length: 354 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydroorotate dehydrogenase
EC: 1.3.98.1
UniProt: G4VFD7
Ligands: QLA, FMN
Pockets: 2 · best druggability 0.84

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydroorotate dehydrogenase (EC 1.3.98.1)	protein	354	40% helix, 16% strand	G4VFD7

Ligands and binding sites

QLA · 2-[(4-fluorophenyl)amino]-3-hydroxynaphthalene-1,4-dione · ligand · chains A
FMN · Flavin mononucleotide · ligand · chains A
GOL · Glycerol · additive · 4 copies · chains A

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

Pockets

2 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	1114	0.84	0.85	110	QLA, GOL, FMN
2	72	0.38	0.79	24	empty

Compared structures

6UY4 · Crystal structure of dihydroorotate dehydrogenase from Schistosoma mansoni · 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 G4VFD7
Elsewhere: RCSB PDB 6UY4 · PDBe 6UY4 · UniProt G4VFD7

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