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Crystal structure of octaprenyl pyrophosphate synthase from hyperthermophilic thermotoga maritima F132A mutant

Analyse Crystal structure of octaprenyl pyrophosphate synthase from hyperthermophilic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1V4I
Type: protein
Length: 279 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Octoprenyl-diphosphate synthase
EC: 2.5.1.11
UniProt: Q9X1M1
Ligands: SO4
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Octoprenyl-diphosphate synthase (EC 2.5.1.11)	protein	279	75% helix, 1% strand	Q9X1M1

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · 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	398	0.69	0.81	45	SO4
2	108	0.48	0.80	22	SO4
3	157	0.48	0.76	17	empty

Compared structures

1V4I · Crystal Structure of Octaprenyl Pyrophosphate Synthase from Hyperthermophilic Thermotoga… · 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 Q9X1M1
Elsewhere: RCSB PDB 1V4I · PDBe 1V4I · UniProt Q9X1M1

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