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Crystal structure of dihydrofolate reductase from mycobacterium tuberculosis in complex with cycloguanil

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

PDB: 4KNE
Type: protein
Length: 318 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: P0A546
Ligands: 1CY, ATR
Pockets: 3 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dihydrofolate reductase (EC 1.5.1.3)	protein	159	19% helix, 34% strand	P0A546

Ligands and binding sites

1CY · 1-(4-chlorophenyl)-6,6-dimethyl-1,6-dihydro-1,3,5-triazine-2,4-diamine · ligand · 2 copies · chains A, B
ATR · 2'-monophosphoadenosine-5'-diphosphate · ligand · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	419	0.66	0.79	37	1CY, ATR
2	360	0.63	0.78	31	1CY
3	75	0.32	0.75	17	ATR

Compared structures

4KNE · Crystal structure of dihydrofolate reductase from Mycobacterium tuberculosis in complex… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt P0A546
Elsewhere: RCSB PDB 4KNE · PDBe 4KNE · UniProt P0A546

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