Research workbench

Crystal structure of epi-isozizaene synthase from streptomyces coelicolor A3(2)

Analyse Crystal structure of epi-isozizaene synthase from streptomyces coelicolor A3(2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LTV
Type: protein
Length: 314 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Epi-isozizaene synthase
EC: 4.2.3.37
UniProt: Q9K499
Ligands: SO4
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Epi-isozizaene synthase (EC 4.2.3.37)	protein	314	75% helix, 0% strand	Q9K499

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A

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	445	0.70	0.81	32	empty

Compared structures

4LTV · Crystal structure of epi-isozizaene synthase from Streptomyces coelicolor A3(2) · the same entry in another collection · chain A against A, TM-score 1.00
Q9K499 · AlphaFold monomer V2.0 prediction for epi-isozizaene synthase (Q9K499) · a predicted model of the same protein · chain A 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 Q9K499
Elsewhere: RCSB PDB 4LTV · PDBe 4LTV · UniProt Q9K499

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