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Crystal structure of the laminarinase catalytic domain from thermotoga maritima MSB8

Analyse Crystal structure of the laminarinase catalytic domain from thermotoga maritima… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3AZX
Type
protein
Length
504 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Laminarinase
EC
3.2.1.39
UniProt
Q9WXN1
Ligands
CA
Pockets
2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BLaminarinase (EC 3.2.1.39)protein2528% helix, 50% strandQ9WXN1

Ligands and binding sites

  • CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15630.680.7862empty
22420.600.7933empty

Interfaces

1 interface between chains.

  • A–B · 716 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 3AZX · Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 · the same entry in another collection · chain A against A, TM-score 1.00

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