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Pandda analysis group deposition -- crystal structure of T. cruzi fpps in complex with FMOPL000416A

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: 5QPV
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: LWA, ZN, SO4
Pockets: 2 · best druggability 0.80

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Farnesyl diphosphate synthase	protein	360	74% helix, 1% strand	Q8WS26

Ligands and binding sites

LWA · (2~{S})-~{N}-(4-aminocarbonylphenyl)oxolane-2-carboxamide · ligand · 2 copies · chains A
ZN · Zinc ion · metal · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	768	0.80	0.83	67	SO4, ZN, LWA
2	68	0.36	0.77	10	empty

Compared structures

5QPV · 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

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 Q8WS26
Elsewhere: RCSB PDB 5QPV · PDBe 5QPV · UniProt Q8WS26

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