MolNFT v1 · #104794 · protein

Crystal structure of I14G DHFR mutant complexed with folate and NADP+

4QLF · Dihydrofolate reductase: “Crystal structure of I14G DHFR mutant complexed with folate and NADP+”. X-ray diffraction, 2 ligands (FOL, NAP), 1 pocket (best druggability 0.61). MolNFT v1 #104794 on GenesisL1: 3D structure, binding…

PDB: 4QLF
Type: protein
Length: 157 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: U6N356
Ligands: FOL, NAP
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	157	25% helix, 38% strand	U6N356

Ligands and binding sites

FOL · Folic acid · 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	409	0.61	0.76	37	FOL

Compared structures

4QLF · Crystal structure of I14G DHFR mutant complexed with folate and NADP+ · 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 U6N356
Elsewhere: RCSB PDB 4QLF · PDBe 4QLF · UniProt U6N356

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