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MolNFT v1 · #37387 · protein

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

2FZN · Bifunctional protein puta, proline dehydrogenase (ec…: “Structure of the E. COLI puta proline dehydrogenase domain reduced by dithionite and complexed with proline”. X-ray diffraction, 2 ligands (FAD, PRO), 4 pockets (best…

PDB
2FZN
Type
protein
Length
449 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, PRO
Pockets
4 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABifunctional protein puta, proline dehydrogenase (ec 1.5.99.8) (proline oxidase) (EC 1.5.99.8)protein44955% helix, 10% strandP09546

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · chains A
  • PRO · Proline · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14660.840.9141FAD, PRO
21660.510.7823empty
31010.440.7924empty
4560.310.7613empty

Compared structures

  • 2FZN · 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 0.92

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