MolNFT v1 · #4796 · protein

The structure of pneumocystis carinii dihydrofolate reductase to 1.9 ångströms resolution

1DYR: “The structure of pneumocystis carinii dihydrofolate reductase to 1.9 ångströms resolution”. X-ray diffraction, 2 ligands (NDP, TOP), 1 pocket (best druggability 0.74). MolNFT v1 #4796 on GenesisL1: 3D structure, binding sites and…

PDB: 1DYR
Type: protein
Length: 205 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: P16184
Ligands: NDP, TOP
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	205	25% helix, 30% strand	P16184

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
TOP · Trimethoprim · 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	504	0.74	0.82	49	NDP, TOP

Compared structures

1DYR · The structure of pneumocystis carinii dihydrofolate reductase to 1.9 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
P16184 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P16184) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P16184
Elsewhere: RCSB PDB 1DYR · PDBe 1DYR · UniProt P16184

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