MolNFT v1 · #63979 · protein

Staphylococcus aureus dihydrofolate reductase complexed with NADPH and 2,4-diamino-5-(3-(2,5-DIMETHOXYPHENYL)PROP-1-ynyl)-6-ethylpyrimidine (UCP120B)

3FQ0 · Trimethoprim-sensitive dihydrofolate reductase: “Staphylococcus aureus dihydrofolate reductase complexed with NADPH and…”. X-ray diffraction, 2 ligands (NDP, N22), 1 pocket (best druggability 0.70). MolNFT v1 #63979 on GenesisL1: 3D…

PDB: 3FQ0
Type: protein
Length: 157 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Trimethoprim-sensitive dihydrofolate reductase
EC: 1.5.1.3
UniProt: Q2YY41
Ligands: NDP, N22
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Trimethoprim-sensitive dihydrofolate reductase (EC 1.5.1.3)	protein	157	20% helix, 36% strand	Q2YY41

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
N22 · 5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine · 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	339	0.70	0.83	38	NDP, N22

Compared structures

3FQ0 · Staphylococcus aureus dihydrofolate reductase complexed with NADPH and… · 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 Q2YY41
Elsewhere: RCSB PDB 3FQ0 · PDBe 3FQ0 · UniProt Q2YY41

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