MolNFT v1 · #132306 · protein

T. brucei fpps in complex with cid 3599333

5QT4 · Farnesyl pyrophosphate synthase: “T. brucei fpps in complex with cid 3599333”. X-ray diffraction, 1 ligand (P9Y), 3 pockets (best druggability 0.66). MolNFT v1 #132306 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5QT4
Type: protein
Length: 325 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Farnesyl pyrophosphate synthase
UniProt: Q86C09
Ligands: P9Y
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	325	78% helix, 0% strand	Q86C09

Ligands and binding sites

P9Y · 1-[3-(4-chlorophenoxy)propyl]-1H-imidazole · ligand · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A
DMS · Dimethyl sulfoxide · 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	478	0.66	0.78	55	P9Y, DMS
2	75	0.39	0.78	16	empty
3	57	0.35	0.78	20	empty

Compared structures

5QT4 · T. brucei FPPS in complex with CID 3599333 · 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 5QT4 · PDBe 5QT4 · UniProt Q86C09

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