MolNFT v2 · #220236 · protein

F96H epi-Isozizaene Synthase: complex with 3 Mg2+ and pamidronate

8SU1: “F96H epi-Isozizaene Synthase: complex with 3 Mg2+ and pamidronate”. X-ray diffraction at 1.37, 3 ligands (210, MG, SO4), 4 pockets (best druggability 0.83). MolNFT v2 #220236 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 8SU1
Type: protein
Length: 340 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.37
Source: Streptomyces coelicolor A3(2)
Molecule: Epi-isozizaene synthase
EC: 4.2.3.37
UniProt: Q9K499
Ligands: 210, MG, SO4
Pockets: 4 · best druggability 0.83

Structure

x-ray diffraction · resolution 1.37 · 1 distinct chain · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Epi-isozizaene synthase (EC 4.2.3.37)	protein	340	76% helix, 0% strand	Q9K499

Ligands and binding sites

210 · Pamidronate · ligand · chains A
MG · Magnesium ion · metal · 3 copies · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

4 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	187	0.83	0.97	39	MG, 210
2	74	0.46	0.82	17	empty
3	51	0.34	0.79	13	SO4
4	66	0.28	0.73	13	empty

Compared structures

Q9K499 · AlphaFold monomer V2.0 prediction for epi-isozizaene synthase (Q9K499) · a predicted model of the same protein · 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 Q9K499
Elsewhere: RCSB PDB 8SU1 · PDBe 8SU1 · UniProt Q9K499

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