MolNFT v1 · #102620 · protein

Klebsiella pneumoniae dihydrofolate reductase complexed with NADPH and 6-ethyl-5-{3-[3-(pyrimidin-5-YL)PHENYL]PROP-1-yn-1-YL}PYRIMIDINE-2,4- diamine

4OR7: “Klebsiella pneumoniae dihydrofolate reductase complexed with NADPH and…”. X-ray diffraction, 2 ligands (NAP, 25U), 1 pocket (best druggability 0.65). MolNFT v1 #102620 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4OR7
Type: protein
Length: 165 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: U5M636
Ligands: NAP, 25U
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	165	25% helix, 33% strand	U5M636

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
25U · 6-ethyl-5-{3-[3-(pyrimidin-5-yl)phenyl]prop-1-yn-1-yl}pyrimidine-2,4-diamine · 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	334	0.65	0.80	42	NAP, 25U

Compared structures

4OR7 · Klebsiella pneumoniae dihydrofolate reductase complexed with NADPH and… · 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 U5M636
Elsewhere: RCSB PDB 4OR7 · PDBe 4OR7 · UniProt U5M636

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