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F96M epi-isozizaene synthase: complex with 3 MG2+ and risedronate

Analyse F96M epi-isozizaene synthase: complex with 3 MG2+ and risedronate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7KJD
Type: protein
Length: 340 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: A0A6M9XZI2
Ligands: RIS, MG, SO4
Pockets: 3 · best druggability 0.84

Structure

x-ray diffraction · 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	A0A6M9XZI2

Ligands and binding sites

RIS · 1-hydroxy-2-(3-pyridinyl)ethylidene bis-phosphonic acid · 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

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	212	0.84	0.97	42	MG, RIS
2	58	0.44	0.83	17	empty
3	64	0.32	0.75	13	empty

Compared structures

7KJD · F96M epi-isozizaene synthase: complex with 3 Mg2+ and risedronate · 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 A0A6M9XZI2
Elsewhere: RCSB PDB 7KJD · PDBe 7KJD · UniProt A0A6M9XZI2

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