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Crystal structure of human fpps in complex with pamidronate

Analyse Crystal structure of human fpps in complex with pamidronate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2F89
Type: protein
Length: 346 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Farnesyl diphosphate synthase
EC: 2.5.1.1, 2.5.1.10
UniProt: P14324
Ligands: 210, MN, PO4
Pockets: 1 · best druggability 0.79

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
F	Farnesyl diphosphate synthase (EC 2.5.1.1, 2.5.1.10)	protein	346	74% helix, 1% strand	P14324

Ligands and binding sites

210 · Pamidronate · ligand · chains F
MN · Manganese (II) ion · metal · 3 copies · chains F
PO4 · Phosphate ion · ion · chains F

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	356	0.79	0.89	59	PO4, MN, 210

Compared structures

2F89 · Crystal structure of human FPPS in complex with pamidronate · the same entry in another collection · chain F against F, TM-score 1.00
P14324 · AlphaFold monomer V2.0 prediction for farnesyl pyrophosphate synthase (P14324) · a predicted model of the same protein · chain F against A, TM-score 0.99

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 P14324
Elsewhere: RCSB PDB 2F89 · PDBe 2F89 · UniProt P14324

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