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Crystal structure of BUGH2AWT in complex with galactoisofagomine

Analyse Crystal structure of BUGH2AWT in complex with galactoisofagomine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5T99
Type: protein
Length: 1,513 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase
Ligands: GIF
Pockets: 19 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase	protein	757	14% helix, 40% strand	—
B	Glycoside hydrolase	protein	756	15% helix, 41% strand	—

Ligands and binding sites

GIF · D-galacto-isofagomine · ligand · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 22 copies · chains A, B

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

Pockets

19 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	107	0.79	0.98	27	empty
2	100	0.78	0.98	27	empty
3	574	0.73	0.81	56	empty
4	429	0.72	0.83	39	empty
5	52	0.71	0.99	23	EDO

Interfaces

1 interface between chains.

A–B · 61 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5T99 · Crystal structure of BuGH2Awt in complex with Galactoisofagomine · 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 5T99 · PDBe 5T99

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