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The GH127, beta-arabinofuranosidase, BT3674

Analyse The GH127, beta-arabinofuranosidase, BT3674 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EX6
Type: protein
Length: 1,267 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Six-hairpin glycosidase
UniProt: Q8A1I7
Ligands: ZN
Pockets: 9 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Six-hairpin glycosidase	protein	633	38% helix, 22% strand	Q8A1I7
A	Six-hairpin glycosidase	protein	634	37% helix, 23% strand	Q8A1I7

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains B, 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, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	468	0.76	0.84	30	empty
2	481	0.75	0.83	30	empty
3	1047	0.72	0.76	80	empty
4	78	0.54	0.85	20	empty
5	75	0.51	0.84	18	empty

Interfaces

1 interface between chains.

B–A · 321 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6EX6 · The GH127, Beta-arabinofuranosidase, BT3674 · the same entry in another collection · chain B against B, 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 Q8A1I7
Elsewhere: RCSB PDB 6EX6 · PDBe 6EX6 · UniProt Q8A1I7

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