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The high resolution structure of a novel alpha-L-arabinofuranosidase (CTGH43) from clostridium thermocellum atcc 27405

Analyse The high resolution structure of a novel alpha-L-arabinofuranosidase (CTGH43)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5A8D
Type: protein
Length: 302 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbohydrate binding family 6
EC: 3.2.1.55
UniProt: A3DEX4
Ligands: SO4
Pockets: 2 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carbohydrate binding family 6 (EC 3.2.1.55)	protein	302	4% helix, 44% strand	A3DEX4

Ligands and binding sites

SO4 · Sulfate ion · ion · 5 copies · chains A
GOL · Glycerol · additive · 4 copies · chains A
ACT · Acetate ion · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	136	0.58	0.83	17	empty
2	230	0.56	0.78	22	GOL

Compared structures

5A8D · The high resolution structure of a novel alpha-L-arabinofuranosidase (CtGH43) from… · 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 A3DEX4
Elsewhere: RCSB PDB 5A8D · PDBe 5A8D · UniProt A3DEX4

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