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Crystal structure of the GH31 alpha-xylosidase (XAC1773) from xanthomonas citri

Analyse Crystal structure of the GH31 alpha-xylosidase (XAC1773) from xanthomonas citri in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7KNC
Type: protein
Length: 919 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-xylosidase
UniProt: Q8PLM2
Ligands: XYS, K
Pockets: 9 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-xylosidase	protein	919	20% helix, 33% strand	Q8PLM2

Ligands and binding sites

XYS · alpha-D-xylopyranose · sugar · chains A
K · Potassium ion · metal · chains A
GOL · Glycerol · additive · 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, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	217	0.73	0.88	41	empty
2	372	0.72	0.83	58	XYS
3	265	0.69	0.84	47	empty
4	98	0.63	0.88	27	empty
5	152	0.59	0.84	24	empty

Compared structures

7KNC · Crystal structure of the GH31 alpha-xylosidase (Xac1773) from Xanthomonas citri · 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 Q8PLM2
Elsewhere: RCSB PDB 7KNC · PDBe 7KNC · UniProt Q8PLM2

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