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Pandda analysis group deposition -- crystal structure of T. cruzi fpps in complex with PKTTA024495B

Analyse Pandda analysis group deposition -- crystal structure of T. cruzi fpps in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5QQ5
Type: protein
Length: 360 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Farnesyl diphosphate synthase
UniProt: Q8WS26
Ligands: JJM, ZN, SO4
Pockets: 3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 74% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Farnesyl diphosphate synthase	protein	360	74% helix, 2% strand	Q8WS26

Ligands and binding sites

JJM · 1-methyl-N-(3-methylphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine · ligand · chains A
ZN · Zinc ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A
ACT · Acetate ion · additive · chains A

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	636	0.77	0.83	55	SO4, ZN
2	50	0.55	0.90	15	empty
3	52	0.35	0.78	10	JJM

Compared structures

5QQ5 · PanDDA analysis group deposition -- Crystal Structure of T. cruzi FPPS in complex with… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8WS26
Elsewhere: RCSB PDB 5QQ5 · PDBe 5QQ5 · UniProt Q8WS26

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