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Crystal structure of fructosyltransferase (D191A) from a. japonicus in complex with raffinose

Analyse Crystal structure of fructosyltransferase (D191A) from a. japonicus in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LIH
Type: protein
Length: 634 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructosyltransferase
Ligands: FRU, GLC, GLA
Pockets: 9 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructosyltransferase	protein	634	9% helix, 43% strand	—

Ligands and binding sites

FRU · beta-D-fructofuranose · sugar · chains A
GLC · alpha-D-glucopyranose · sugar · chains A
GLA · alpha-D-galactopyranose · sugar · chains A

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

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	67	0.76	0.99	20	empty
2	428	0.69	0.80	37	FRU, GLC, GLA
3	205	0.61	0.82	28	empty
4	139	0.41	0.75	30	empty
5	82	0.36	0.76	19	empty

Compared structures

3LIH · Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with… · 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 3LIH · PDBe 3LIH

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