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T. brucei fpps in complex with 1-((1H-indol-3-YL)METHYL)-N-(3- CHLOROBENZYL)PIPERIDIN-4-amine

Analyse T. brucei fpps in complex with 1-((1H-indol-3-YL)METHYL)-N-(3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SII
Type: protein
Length: 328 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Farnesyl pyrophosphate synthase
UniProt: Q86C09
Ligands: LEZ
Pockets: 3 · best druggability 0.61

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Farnesyl pyrophosphate synthase	protein	328	78% helix, 0% strand	Q86C09

Ligands and binding sites

LEZ · ~{N}-[(3-chlorophenyl)methyl]-1-(1~{H}-indol-3-ylmethyl)piperidin-4-amine · ligand · 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	429	0.61	0.76	52	LEZ
2	65	0.36	0.78	18	empty
3	60	0.34	0.77	11	GOL

Compared structures

6SII · T. brucei FPPS in complex with 1-((1H-indol-3-yl)methyl)-N-(3-chlorobenzyl)piperidin-4-ami… · 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 6SII · PDBe 6SII · UniProt Q86C09

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