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Crystal structure of carbohydrate esterase pbeacxe, apoenzyme

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

PDB
7TOG
Type
protein
Length
378 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sgnh hydrolase
UniProt
A0A5M4AV20
Pockets
3 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASgnh hydrolaseprotein37826% helix, 32% strandA0A5M4AV20

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1970.390.7730empty
2670.360.7817empty
3680.320.7517empty

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

  • 7TOG · Crystal structure of carbohydrate esterase PbeAcXE, apoenzyme · the same entry in another collection · chain A against A, TM-score 1.00

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