MolNFT v1 · #52729 · protein

Wild-type staphylococcus aureus DHFR in complex with NADPH and trimethoprim

2W9G · Dihydrofolate reductase: “Wild-type staphylococcus aureus DHFR in complex with NADPH and trimethoprim”. X-ray diffraction, 2 ligands (TOP, NDP), 1 pocket (best druggability 0.69). MolNFT v1 #52729 on GenesisL1: 3D structure, binding…

PDB: 2W9G
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: P0A017
Ligands: TOP, NDP
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	157	20% helix, 36% strand	P0A017

Ligands and binding sites

TOP · Trimethoprim · 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	338	0.69	0.82	36	TOP, NDP

Compared structures

2W9G · Wild-type Staphylococcus aureus DHFR in complex with NADPH and trimethoprim · the same entry in another collection · chain A against A, TM-score 1.00
P0A017 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P0A017) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P0A017
Elsewhere: RCSB PDB 2W9G · PDBe 2W9G · UniProt P0A017

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