Research workbench

T. brucei FPPS in complex with CID 23155989

Analyse T. brucei FPPS in complex with CID 23155989 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5QT9
Type: protein
Length: 325 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.199
Source: Trypanosoma brucei
Molecule: Farnesyl pyrophosphate synthase
UniProt: Q86C09
Ligands: PJ4
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · resolution 2.199 · 1 distinct chain · 79% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Farnesyl pyrophosphate synthase	protein	325	79% helix, 0% strand	Q86C09

Ligands and binding sites

PJ4 · (1S)-3-chloro-1-(4-methylpiperazin-1-yl)-1,4-dihydroisoquinoline · 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

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	482	0.62	0.76	51	DMS
2	60	0.35	0.78	11	empty

Compared structures

5QT9 · T. brucei fpps in complex with cid 23155989 · 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 5QT9 · PDBe 5QT9 · UniProt Q86C09

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.