Research workbench

Fusidic acid resistance protein fusb

Analyse Fusidic acid resistance protein fusb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ADO
Type: protein
Length: 412 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FAR1
UniProt: Q8GNY5
Ligands: ZN
Pockets: 5 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FAR1	protein	209	44% helix, 21% strand	Q8GNY5
B	FAR1	protein	203	46% helix, 19% strand	Q8GNY5

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1042	0.82	0.83	75	empty
2	158	0.54	0.80	19	empty
3	152	0.50	0.78	19	empty
4	112	0.38	0.74	20	empty
5	59	0.35	0.78	11	empty

Interfaces

1 interface between chains.

A–B · 1253 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

4ADO · Fusidic acid resistance protein FusB · 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 Q8GNY5
Elsewhere: RCSB PDB 4ADO · PDBe 4ADO · UniProt Q8GNY5

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