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Beta-glucosidase a from the halothermophile H. orenii

Analyse Beta-glucosidase a from the halothermophile H. orenii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TA9
Type: protein
Length: 889 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase family 1
EC: 3.2.1.21
UniProt: B8CYA8
Ligands: NI
Pockets: 6 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase family 1 (EC 3.2.1.21)	protein	448	43% helix, 17% strand	B8CYA8
B	Glycoside hydrolase family 1 (EC 3.2.1.21)	protein	441	43% helix, 17% strand	B8CYA8

Ligands and binding sites

NI · Nickel (II) ion · metal · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	365	0.81	0.90	45	empty
2	664	0.72	0.79	64	NI
3	513	0.70	0.79	43	NI
4	151	0.45	0.76	23	empty
5	143	0.44	0.76	21	empty

Interfaces

1 interface between chains.

A–B · 545 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

3TA9 · beta-Glucosidase A from the halothermophile H. orenii · 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 B8CYA8
Elsewhere: RCSB PDB 3TA9 · PDBe 3TA9 · UniProt B8CYA8

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