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Crystal Structure of Extra C-terminal Domain (X) of Exo-1,3/1,4-beta-glucanase (ExoP) from Pseudoalteromonas sp. BB1

Analyse Crystal Structure of Extra C-terminal Domain (X) of Exo-1,3/1,4-beta-glucanase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3F95
Type: protein
Length: 348 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.8
Source: Pseudoalteromonas sp.
Molecule: Beta-glucosidase
UniProt: Q0QJA3
Ligands: CL
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · resolution 1.8 · 2 distinct chains · 6% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-glucosidase	protein	175	6% helix, 55% strand	Q0QJA3
B	Beta-glucosidase	protein	173	6% helix, 55% strand	Q0QJA3

Ligands and binding sites

CL · Chloride ion · ion · 5 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	250	0.54	0.77	45	empty

Interfaces

1 interface between chains.

A–B · 544 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3F95 · Crystal structure of extra C-terminal domain (X) of exo-1,3/1,4-beta- glucanase (exop)… · 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 Q0QJA3
Elsewhere: RCSB PDB 3F95 · PDBe 3F95 · UniProt Q0QJA3

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