MolNFT v1 · #99587 · protein

Dihydrofolate reductase from enterococcus faecalis complexed with NADP(H)AND rab-propyl

4M7V: “Dihydrofolate reductase from enterococcus faecalis complexed with NADP(H)AND rab-propyl”. X-ray diffraction, 2 ligands (RAR, NAP), 1 pocket (best druggability 0.65). MolNFT v1 #99587 on GenesisL1: 3D structure, binding sites and…

PDB: 4M7V
Type: protein
Length: 168 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: Q834R2
Ligands: RAR, NAP
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	168	24% helix, 33% strand	Q834R2

Ligands and binding sites

RAR · 5-(3,4-dimethoxy-5-{(1E)-3-oxo-3-[(1S)-1-propylphthalazin-2(1H)-yl]prop-1-en-1-yl}benzyl)pyrimidine-2,4-diamine · ligand · chains A
NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · 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	263	0.65	0.82	40	RAR, NAP

Compared structures

4M7V · Dihydrofolate reductase from Enterococcus faecalis complexed with NADP(H)and RAB-propyl · 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 Q834R2
Elsewhere: RCSB PDB 4M7V · PDBe 4M7V · UniProt Q834R2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.