Research workbench

S. aureus mepr F27L mutant bound to oligodeoxyribonucleotide

Analyse S. aureus mepr F27L mutant bound to oligodeoxyribonucleotide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FB2
Type: protein + DNA
Length: 143 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Marr family regulatory protein; DNA (5'-D(*CP*GP*TP*TP*A)-3')
UniProt: Q5Y812
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 68% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Marr family regulatory protein	protein	138	68% helix, 12% strand	Q5Y812
B	DNA (5'-D(CPGPTPTP*A)-3')	dna	5	—	—

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	105	0.37	0.73	17	empty

Interfaces

1 interface between chains.

A–B · 492 Å² buried · 6 hydrogen bonds · protein-nucleic

Compared structures

5FB2 · S. aureus MepR F27L Mutant bound to oligodeoxyribonucleotide · 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 5FB2 · PDBe 5FB2 · UniProt Q5Y812

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