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Structure of the dihydrofolate reductase (fola) from coxiella burnetii in complex with trimethoprim

Analyse Structure of the dihydrofolate reductase (fola) from coxiella burnetii in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TQ8
Type: protein
Length: 171 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: Q83AB2
Ligands: NDP, TOP
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	171	20% helix, 35% strand	Q83AB2

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
TOP · Trimethoprim · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	397	0.69	0.81	44	NDP, TOP

Compared structures

3TQ8 · Structure of the dihydrofolate reductase (folA) from Coxiella burnetii in complex with… · 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 Q83AB2
Elsewhere: RCSB PDB 3TQ8 · PDBe 3TQ8 · UniProt Q83AB2

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