Research workbench

A CBM32 derived from alginate lyase B (AlyB-OU02)

Analyse A CBM32 derived from alginate lyase B (AlyB-OU02) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZU6
Type: protein
Length: 152 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.4
Source: Vibrio
Molecule: CBM32 domain
Ligands: NA
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · resolution 1.4 · 1 distinct chain · 5% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CBM32 domain	protein	152	5% helix, 49% strand	—

Ligands and binding sites

NA · Sodium ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	68	0.37	0.78	18	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5ZU6 · A CBM32 derived from alginate lyase B (alyb-OU02) · 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
Elsewhere: RCSB PDB 5ZU6 · PDBe 5ZU6

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.