Research workbench

E. COLI dihydroorotate dehydrogenase

Analyse E. COLI dihydroorotate dehydrogenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7T6H
Type: protein
Length: 670 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydroorotate dehydrogenase (quinone)
EC: 1.3.5.2
UniProt: P0A7E1
Ligands: ORO, FMN
Pockets: 5 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2)	protein	335	41% helix, 18% strand	P0A7E1

Ligands and binding sites

ORO · Orotic acid · ligand · 2 copies · chains A, B
FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	502	0.82	0.88	69	ORO, FMN
2	540	0.81	0.87	78	ORO, FMN
3	576	0.69	0.78	38	empty
4	78	0.33	0.74	21	empty
5	54	0.31	0.77	13	empty

Interfaces

1 interface between chains.

A–B · 996 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

7T6H · E. coli dihydroorotate dehydrogenase · the same entry in another collection · chain A against A, TM-score 1.00
P0A7E1 · AlphaFold monomer V2.0 prediction for dihydroorotate dehydrogenase (quinone) (P0A7E1) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P0A7E1
Elsewhere: RCSB PDB 7T6H · PDBe 7T6H · UniProt P0A7E1

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