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Dihydrofolate reductase (DHFR) of aspergillus flavus in complex with a small molecule inhibitor

Analyse Dihydrofolate reductase (DHFR) of aspergillus flavus in complex with a small… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6DTC
Type: protein
Length: 244 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
UniProt: B8NBN5
Ligands: NAP, H9G, SO4
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase	protein	244	34% helix, 30% strand	B8NBN5

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
H9G · (3R)-3-methyl-4-[3-(1H-tetrazol-5-yl)phenoxy]-2,3-dihydrofuro[2,3-f]quinazoline-7,9-diamine · ligand · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	418	0.70	0.81	43	NAP, H9G
2	115	0.43	0.77	26	empty

Compared structures

6DTC · Dihydrofolate Reductase (DHFR) of Aspergillus flavus in complex with a small molecule… · 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 B8NBN5
Elsewhere: RCSB PDB 6DTC · PDBe 6DTC · UniProt B8NBN5

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