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Structure of 15, 16- DIHYDROBILIVERDIN:FERREDOXIN oxidoreductase (peba)

Analyse Structure of 15, 16- DIHYDROBILIVERDIN:FERREDOXIN oxidoreductase (peba) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2X9O
Type
protein
Length
233 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
15,16-dihydrobiliverdin-ferredoxin oxidoreductase
EC
1.3.7.2
UniProt
Q02189
Ligands
BLA
Pockets
2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A15,16-dihydrobiliverdin-ferredoxin oxidoreductase (EC 1.3.7.2)protein23342% helix, 25% strandQ02189

Ligands and binding sites

  • BLA · Biliverdine IX alpha · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13310.770.8738BLA
2510.280.7513empty

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

  • 2X9O · STRUCTURE OF 15, 16- DIHYDROBILIVERDIN:FERREDOXIN OXIDOREDUCTASE (PebA) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q02189 · AlphaFold monomer V2.0 prediction for 15,16-DIHYDROBILIVERDIN:FERREDOXIN oxidoreductase… · a predicted model of the same protein · chain A against A, TM-score 0.99

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