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Crystal structure of GH9 exo-beta-D-glucosaminidase PBPRA0520

Analyse Crystal structure of GH9 exo-beta-D-glucosaminidase PBPRA0520 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5DGQ
Type
protein
Length
1,151 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative endoglucanase-related protein
UniProt
Q6LUT2
Ligands
NA
Pockets
10 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative endoglucanase-related proteinprotein57840% helix, 16% strandQ6LUT2
BPutative endoglucanase-related proteinprotein57340% helix, 16% strandQ6LUT2

Ligands and binding sites

  • NA · Sodium ion · metal · 2 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17300.760.8160empty
2730.740.9824empty
3750.730.9725empty
49180.710.7683empty
52120.670.8525empty

Interfaces

1 interface between chains.

  • A–B · 1532 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 5DGQ · Crystal structure of GH9 exo-beta-D-glucosaminidase PBPRA0520 · the same entry in another collection · chain A against A, TM-score 1.00

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