MolNFT v1 · #80221 · protein

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

3TQB: “Structure of the dihydrofolate reductase (fola) from coxiella burnetii in complex with folate”. X-ray diffraction, 2 ligands (NDP, FOL), 1 pocket (best druggability 0.71). MolNFT v1 #80221 on GenesisL1: 3D structure, binding sites…

PDB: 3TQB
Type: protein
Length: 151 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, FOL
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	151	25% helix, 34% strand	Q83AB2

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
FOL · Folic acid · 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	432	0.71	0.82	44	NDP, FOL

Compared structures

3TQB · 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 3TQB · PDBe 3TQB · UniProt Q83AB2

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