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X-ray structure of glucuronoxylan-xylanohydrolase (XYN30A) from clostridium thermocellum at 1.68 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: 4UQB
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: SO4
Pockets: 2 · best druggability 0.31

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

SO4 · Sulfate ion · ion · 2 copies · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · 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	62	0.31	0.75	18	empty
2	68	0.29	0.73	13	EPE

Compared structures

4UQB · 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 4UQB · PDBe 4UQB · UniProt E6UTM3

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