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Crystal structure of the GH35 beta-galactosidase (XAC1772) from xanthomonas citri in complex with galactose

Analyse Crystal structure of the GH35 beta-galactosidase (XAC1772) from xanthomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7KMO
Type: protein
Length: 511 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-galactosidase, GH35
UniProt: Q8PLM3
Ligands: GLA, SO4
Pockets: 3 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-galactosidase, GH35	protein	511	32% helix, 31% strand	Q8PLM3

Ligands and binding sites

GLA · alpha-D-galactopyranose · sugar · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
GOL · Glycerol · additive · 5 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	136	0.40	0.74	26	GLA
2	80	0.36	0.76	15	empty
3	115	0.35	0.73	17	empty

Compared structures

7KMO · Crystal structure of the GH35 beta-galactosidase (Xac1772) from Xanthomonas citri in… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8PLM3
Elsewhere: RCSB PDB 7KMO · PDBe 7KMO · UniProt Q8PLM3

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