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Crystal structure of mycobacterium tuberculosis dihydrofolate reductase bound to NADP and P65 inhibitor

Analyse Crystal structure of mycobacterium tuberculosis dihydrofolate reductase bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5U27
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: A0A0E8UVJ4
Ligands: NAP, P65
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	166	20% helix, 33% strand	A0A0E8UVJ4

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
P65 · 2,4-diamino-6-methyl-5-[3-(2,4,5-trichlorophenoxy)propyloxy]pyrimidine · ligand · chains A
EDO · 1,2-ethanediol · additive · 3 copies · 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	470	0.75	0.84	51	NAP, EDO, P65

Compared structures

5U27 · Crystal Structure of Mycobacterium tuberculosis Dihydrofolate Reductase Bound to NADP 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 A0A0E8UVJ4
Elsewhere: RCSB PDB 5U27 · PDBe 5U27 · UniProt A0A0E8UVJ4

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