Research workbench

Staphylococcus aureus FUSB:EF-GC3 complex

Analyse Staphylococcus aureus FUSB:EF-GC3 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2MZW
Type: protein
Length: 505 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elongation factor G; FAR1
UniProt: W8UT26, Q8GNY5
Ligands: ZN
Pockets: 6 · best druggability 0.81

Structure

solution nmr · 2 distinct chains · 35% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Elongation factor G	protein	292	32% helix, 28% strand	W8UT26
B	FAR1	protein	213	40% helix, 19% strand	Q8GNY5

Ligands and binding sites

ZN · Zinc ion · metal · chains B

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	661	0.81	0.85	71	empty
2	933	0.75	0.78	76	empty
3	173	0.51	0.78	23	empty
4	131	0.43	0.76	25	empty
5	129	0.36	0.72	23	empty

Interfaces

1 interface between chains.

A–B · 1501 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

2MZW · Staphylococcus aureus FusB:EF-GC3 complex · 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 W8UT26
Every structure of UniProt Q8GNY5
Elsewhere: RCSB PDB 2MZW · PDBe 2MZW · UniProt W8UT26 · UniProt Q8GNY5

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