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Crystal structure of the ternary mtx NADPH complex of bacillus anthracis dihydrofolate reductase

Analyse Crystal structure of the ternary mtx NADPH complex of bacillus anthracis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DAT
Type: protein
Length: 161 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: Q81R22
Ligands: MTX, NDP
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	161	17% helix, 31% strand	Q81R22

Ligands and binding sites

MTX · Methotrexate · ligand · chains A
NDP · Nadph dihydro-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	403	0.70	0.82	43	MTX, NDP

Compared structures

3DAT · Crystal structure of the ternary MTX NADPH complex of Bacillus anthracis dihydrofolate… · 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 Q81R22
Elsewhere: RCSB PDB 3DAT · PDBe 3DAT · UniProt Q81R22

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