Research workbench

Wild-type SaSQS1 Complexed with Ibandronate

Analyse Wild-type SaSQS1 Complexed with Ibandronate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6O9P
Type: protein
Length: 508 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.1
Source: Santalum album
Molecule: Sesquisabinene B synthase 1
UniProt: A0A0A0RDR2
Ligands: BFQ, MG
Pockets: 5 · best druggability 0.70

Structure

x-ray diffraction · resolution 2.1 · 1 distinct chain · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sesquisabinene B synthase 1	protein	508	73% helix, 0% strand	A0A0A0RDR2

Ligands and binding sites

BFQ · Ibandronate · ligand · chains A
MG · Magnesium ion · metal · 3 copies · chains A
EDO · 1,2-ethanediol · additive · 6 copies · chains A

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	276	0.70	0.85	35	empty
2	426	0.69	0.81	55	BFQ, MG
3	311	0.68	0.82	34	EDO
4	191	0.52	0.77	22	EDO
5	67	0.38	0.79	20	empty

Compared structures

6O9P · Wild-type SASQS1 complexed with ibandronate · 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 A0A0A0RDR2
Elsewhere: RCSB PDB 6O9P · PDBe 6O9P · UniProt A0A0A0RDR2

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