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Structure of BT4661, a suse-like surface located polysaccharide binding protein from the bacteroides thetaiotaomicron heparin utilisation locus

Analyse Structure of BT4661, a suse-like surface located polysaccharide binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AK2
Type: protein
Length: 286 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BT_4661
UniProt: Q89YS0
Ligands: SGN, IDS, NA
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BT_4661	protein	286	13% helix, 34% strand	Q89YS0

Ligands and binding sites

SGN · 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose · sugar · 3 copies · chains A
IDS · 2-O-sulfo-alpha-L-idopyranuronic acid · sugar · 3 copies · chains A
NA · Sodium ion · metal · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	168	0.61	0.83	19	empty
2	146	0.46	0.77	22	empty

Compared structures

4AK2 · Structure of BT4661, a SusE-like surface located polysaccharide binding protein from the… · 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 Q89YS0
Elsewhere: RCSB PDB 4AK2 · PDBe 4AK2 · UniProt Q89YS0

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