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Structure of the E. COLI puta proline dehydrogenase domain reduced by dithionite and complexed with SO2

Analyse Structure of the E. COLI puta proline dehydrogenase domain reduced by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2FZM
Type
protein
Length
450 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Bifunctional protein puta, proline dehydrogenase (ec 1.5.99.8) (proline oxidase)
EC
1.5.99.8
UniProt
P09546
Ligands
FAD, SO2
Pockets
3 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABifunctional protein puta, proline dehydrogenase (ec 1.5.99.8) (proline oxidase) (EC 1.5.99.8)protein45056% helix, 10% strandP09546

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · chains A
  • SO2 · Sulfur dioxide · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14730.840.9143FAD, SO2
21730.520.7825empty
3630.330.7614empty

Compared structures

  • 2FZM · Structure of the E. coli PutA proline dehydrogenase domain reduced by dithionite and… · the same entry in another collection · chain A against A, TM-score 1.00
  • P09546 · AlphaFold monomer V2.0 prediction for bifunctional protein puta (P09546) · a predicted model of the same protein · chain A against A, TM-score 0.91

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