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Structure of a transaldolase from oleispira antarctica

Analyse Structure of a transaldolase from oleispira antarctica in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3M16
Type
protein
Length
326 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transaldolase
EC
2.2.1.-
Pockets
2 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATransaldolase (EC 2.2.1.-)protein32655% helix, 12% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1990.410.7723empty
2770.380.7714empty

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 3M16 · Structure of a Transaldolase from Oleispira antarctica · the same entry in another collection · chain A against A, TM-score 1.00

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