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Crystal structure of AoRut

Analyse Crystal structure of AoRut in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LA0
Type: protein
Length: 720 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.75
Source: Aspergillus oryzae
Molecule: Glycoside hydrolase family 5
UniProt: A0A1S9DRB1
Ligands: NAG
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · resolution 1.75 · 1 distinct chain · 42% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glycoside hydrolase family 5	protein	360	42% helix, 15% strand	A0A1S9DRB1

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A, B

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

Pockets

3 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	585	0.68	0.78	83	NAG
2	458	0.67	0.79	53	empty
3	434	0.66	0.79	50	empty

Interfaces

1 interface between chains.

A–B · 591 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 glycan, 2 disulfide (N-glycosylation, disulfide).

Compared structures

6LA0 · Crystal structure of aorut · 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 A0A1S9DRB1
Elsewhere: RCSB PDB 6LA0 · PDBe 6LA0 · UniProt A0A1S9DRB1

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