MolNFT v1 · #179862 · protein

Crystal structure of dihydrofolate reductase (DHFR) from mycobacterium ulcerans AGY99 in complex with NADP and inhibitor sddc-0001912

7KI9: “Crystal structure of dihydrofolate reductase (DHFR) from mycobacterium ulcerans AGY99 in complex with NADP…”. X-ray diffraction, 2 ligands (NAP, WFJ), 1 pocket (best druggability 0.72). MolNFT v1 #179862 on GenesisL1: 3D structure…

PDB: 7KI9
Type: protein
Length: 166 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: A0PQG8
Ligands: NAP, WFJ
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	166	21% helix, 33% strand	A0PQG8

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
WFJ · 1-[2-(3-{[(2,4-diamino-6-ethylpyrimidin-5-yl) oxy]methyl}azetidin-1-yl)phenyl]piperidine-4-carboxylic acid · 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	537	0.72	0.81	48	NAP, WFJ

Compared structures

7KI9 · Crystal Structure of Dihydrofolate reductase (DHFR) from Mycobacterium ulcerans Agy99 in… · 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 A0PQG8
Elsewhere: RCSB PDB 7KI9 · PDBe 7KI9 · UniProt A0PQG8

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