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The crystal structure of a natural product biosynthetic enzyme from streptomyces sp. CB03234

Analyse The crystal structure of a natural product biosynthetic enzyme from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5UHJ
Type
protein
Length
245 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
GLYOXALASE/BLEOMYCIN resisance PROTEIN/DIOXYGENASE
UniProt
A0A125SA24
Pockets
3 · best druggability 0.43

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGLYOXALASE/BLEOMYCIN resisance PROTEIN/DIOXYGENASEprotein12317% helix, 41% strandA0A125SA24
BGLYOXALASE/BLEOMYCIN resisance PROTEIN/DIOXYGENASEprotein12217% helix, 39% strandA0A125SA24

Ligands and binding sites

  • FMT · Formic acid · additive · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11170.430.7723empty
2770.370.7715empty
3880.370.7617empty

Interfaces

1 interface between chains.

  • A–B · 385 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 5UHJ · The crystal structure of a natural product biosynthetic enzyme from Streptomyces sp.… · the same entry in another collection · chain A against A, TM-score 1.00

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