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Structure of a periplasmic oligogalacturonide binding protein from yersinia enterocolitica in complex with 4,5-unsaturated digalacturonic acid

Analyse Structure of a periplasmic oligogalacturonide binding protein from yersinia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2UVI
Type: protein
Length: 404 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ABC type periplasmic sugar-binding protein
Ligands: AQA, ADA
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ABC type periplasmic sugar-binding protein	protein	404	48% helix, 15% strand	—

Ligands and binding sites

AQA · 4-deoxy-beta-L-threo-hex-4-enopyranuronic acid · ligand · chains A
ADA · alpha-D-galactopyranuronic acid · sugar · 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	439	0.72	0.82	52	ADA, AQA
2	101	0.36	0.74	15	empty

Compared structures

2UVI · Structure of a periplasmic oligogalacturonide binding protein from Yersinia… · 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
Elsewhere: RCSB PDB 2UVI · PDBe 2UVI

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