Research workbench

S. aureus mepr G34K mutant

Analyse S. aureus mepr G34K mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FFX
Type: protein
Length: 551 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Marr family regulatory protein
UniProt: Q5Y812
Ligands: SO4
Pockets: 4 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Marr family regulatory protein	protein	138	70% helix, 7% strand	Q5Y812
D	Marr family regulatory protein	protein	137	72% helix, 11% strand	Q5Y812

Ligands and binding sites

SO4 · Sulfate ion · ion · 13 copies · chains A, D, B, C
GOL · Glycerol · additive · 2 copies · chains D, C

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

Pockets

4 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	303	0.58	0.77	32	empty
2	238	0.53	0.76	28	SO4
3	70	0.40	0.79	15	empty
4	91	0.37	0.76	21	empty

Interfaces

2 interfaces between chains.

A–B · 1941 Å² buried · 18 hydrogen bonds · protein-protein
D–C · 1869 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

5FFX · S. aureus MepR G34K Mutant · 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 Q5Y812
Elsewhere: RCSB PDB 5FFX · PDBe 5FFX · UniProt Q5Y812

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