Research workbench

Solution structure of L. casei dihydrofolate reductase complexed with NADPH, 30 structures

Analyse Solution structure of L. casei dihydrofolate reductase complexed with NADPH, 30… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2LF1
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: NDP
Pockets: 2 · best druggability 0.69

Structure

solution nmr · 1 distinct chain · 23% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	162	23% helix, 33% strand	P00381

Ligands and binding sites

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

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	338	0.69	0.82	43	NDP
2	52	0.45	0.84	17	empty

Compared structures

2LF1 · Solution structure of L. casei dihydrofolate reductase complexed with NADPH, 30 structures · 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 0.93

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 2LF1 · PDBe 2LF1 · UniProt P00381

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