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NMR solution structure and dynamics of the complex of lactobacillus casei dihydrofolate reductase with the new lipophilic antifolate drug trimetrexate, 22 structures

Analyse NMR solution structure and dynamics of the complex of lactobacillus casei… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BZF
Type: protein
Length: 162 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: P00381
Ligands: TMQ
Pockets: 1 · best druggability 0.71

Structure

solution nmr · 1 distinct chain · 23% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	162	23% helix, 30% strand	P00381

Ligands and binding sites

TMQ · Trimetrexate · 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	424	0.71	0.81	39	TMQ

Compared structures

1BZF · NMR solution structure and dynamics of the complex of lactobacillus casei dihydrofolate… · the same entry in another collection · chain A against A, TM-score 1.00
P00381 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P00381) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P00381
Elsewhere: RCSB PDB 1BZF · PDBe 1BZF · UniProt P00381

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