Research workbench

Bsha from staphylococcus aureus complexed with udp and N- acetylglucosamine

Analyse Bsha from staphylococcus aureus complexed with udp and N- acetylglucosamine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6N1X
Type: protein
Length: 377 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycosyltransferase
EC: 2.4.1.-
UniProt: T1Y9F7
Ligands: UDP, NDG
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycosyltransferase (EC 2.4.1.-)	protein	377	49% helix, 18% strand	T1Y9F7

Ligands and binding sites

UDP · Uridine-5'-diphosphate · ligand · chains A
NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	741	0.75	0.80	71	UDP, NDG

Compared structures

6N1X · BshA from Staphylococcus aureus complexed with UDP and N-acetylglucosamine · 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 T1Y9F7
Elsewhere: RCSB PDB 6N1X · PDBe 6N1X · UniProt T1Y9F7

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