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Structure of frmsr of staphylococcus aureus (complex with substrate)

Analyse Structure of frmsr of staphylococcus aureus (complex with substrate) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KSG
Type: protein
Length: 306 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein
EC: 1.8.4.14
UniProt: Q6GFY9
Ligands: SME
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative uncharacterized protein (EC 1.8.4.14)	protein	153	35% helix, 26% strand	Q6GFY9

Ligands and binding sites

SME · Methionine sulfoxide · ligand · 2 copies · chains A, B

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

Pockets

2 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	257	0.60	0.80	28	SME
2	274	0.59	0.79	31	SME

Interfaces

1 interface between chains.

A–B · 958 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

3KSG · structure of fRMsr of Staphylococcus aureus (complex with substrate) · 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 Q6GFY9
Elsewhere: RCSB PDB 3KSG · PDBe 3KSG · UniProt Q6GFY9

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