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MolNFT v1 · #37386 · protein

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

2FZM · Bifunctional protein puta, proline dehydrogenase (ec…: “Structure of the E. COLI puta proline dehydrogenase domain reduced by dithionite and complexed with SO2”. X-ray diffraction, 2 ligands (FAD, SO2), 3 pockets (best druggability…

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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