MolNFT v1 · #132318 · protein

T. brucei fpps in complex with cid 126782062

5QTG · Farnesyl pyrophosphate synthase: “T. brucei fpps in complex with cid 126782062”. X-ray diffraction, 3 ligands (PK4, NA, PO4), 3 pockets (best druggability 0.66). MolNFT v1 #132318 on GenesisL1: 3D structure, binding sites and…

PDB: 5QTG
Type: protein
Length: 330 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Farnesyl pyrophosphate synthase
UniProt: Q86C09
Ligands: PK4, NA, PO4
Pockets: 3 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Farnesyl pyrophosphate synthase	protein	330	78% helix, 0% strand	Q86C09

Ligands and binding sites

PK4 · 2-fluoro-N,3-dimethylbenzene-1-sulfonamide · ligand · chains A
NA · Sodium ion · metal · chains A
PO4 · Phosphate ion · ion · 2 copies · chains A
GOL · Glycerol · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	604	0.66	0.76	50	NA, PO4, GOL
2	90	0.46	0.80	14	PK4
3	76	0.35	0.76	22	empty

Compared structures

5QTG · T. brucei FPPS in complex with CID 126782062 · 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 Q86C09
Elsewhere: RCSB PDB 5QTG · PDBe 5QTG · UniProt Q86C09

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