MolNFT v1 · #160673 · protein

S. aureus dihydrofoate reductase co-crystallized with 3,5- dimethylphenyl-dihydropthalazine inhibitor and NADP(H)

6PR8: “S. aureus dihydrofoate reductase co-crystallized with 3,5- dimethylphenyl-dihydropthalazine inhibitor and…”. X-ray diffraction, 2 ligands (OWJ, NAP). MolNFT v1 #160673 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6PR8
Type: protein
Length: 162 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P0A017
Ligands: OWJ, NAP

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	162	—	P0A017

Ligands and binding sites

OWJ · (2E)-3-{5-[(2,4-diaminopyrimidin-5-yl)methyl]-2,3-dimethoxyphenyl}-1-[(1S)-1-(3,5-dimethylphenyl) phthalazin-2(1H)-yl]prop-2-en-1-one · ligand · chains A
NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
GOL · Glycerol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6PR8 · S. aureus dihydrofoate reductase co-crystallized with… · 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 0.97

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 P0A017
Elsewhere: RCSB PDB 6PR8 · PDBe 6PR8 · UniProt P0A017

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