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X-ray structure of glucuronoxylan-xylanohydrolase (XYN30A) from clostridium thermocellum at 1.30 a resolution

Analyse X-ray structure of glucuronoxylan-xylanohydrolase (XYN30A) from clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4UQC
Type: protein
Length: 390 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbohydrate binding family 6
EC: 3.2.1.8
UniProt: E6UTM3
Ligands: GLC
Pockets: 2 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carbohydrate binding family 6 (EC 3.2.1.8)	protein	390	27% helix, 34% strand	E6UTM3

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · chains A
TAR · D(-)-tartaric acid · additive · chains A
TLA · L(+)-tartaric acid · additive · chains A

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

Pockets

2 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	70	0.33	0.76	18	empty
2	61	0.28	0.73	15	GLC

Compared structures

4UQC · X-ray structure of glucuronoxylan-xylanohydrolase (Xyn30A) from Clostridium thermocellum… · 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 E6UTM3
Elsewhere: RCSB PDB 4UQC · PDBe 4UQC · UniProt E6UTM3

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