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The structure of GH26C from muricauda sp. MAR_2010_75

Analyse The structure of GH26C from muricauda sp. MAR_2010_75 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6Q78
Type
protein
Length
748 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
GH26C
EC
3.2.1.78
Pockets
4 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BGH26C (EC 3.2.1.78)protein37439% helix, 15% strand—

Ligands and binding sites

  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13830.600.7650TRS
23760.580.7652TRS
31900.520.7834empty
41560.500.7829empty

Interfaces

1 interface between chains.

  • A–B · 572 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 6Q78 · The structure of GH26C from Muricauda sp. MAR_2010_75 · the same entry in another collection · chain A against A, TM-score 1.00

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