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The crystal structure of the GH30 subfamily 10 enzyme, ACXBH30A from acetivibrio clariflavus in complex with xylobiose

Analyse The crystal structure of the GH30 subfamily 10 enzyme, ACXBH30A from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7N6O
Type: protein
Length: 865 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ACXBH30A
UniProt: G8LU16
Ligands: XYP, CL
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ACXBH30A	protein	433	27% helix, 31% strand	G8LU16
B	ACXBH30A	protein	432	27% helix, 31% strand	G8LU16

Ligands and binding sites

XYP · beta-D-xylopyranose · sugar · 4 copies · chains B, A
CL · Chloride ion · ion · 11 copies · chains A, B

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

Pockets

3 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	725	0.73	0.79	58	XYP
2	249	0.49	0.74	45	CL
3	104	0.49	0.80	18	XYP

Interfaces

1 interface between chains.

A–B · 397 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

7N6O · The crystal structure of the GH30 subfamily 10 enzyme, AcXbh30A from Acetivibrio… · 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 G8LU16
Elsewhere: RCSB PDB 7N6O · PDBe 7N6O · UniProt G8LU16

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