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Crystal structure of radical D105N synechocystis sp. pcya

Analyse Crystal structure of radical D105N synechocystis sp. pcya in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3F0M
Type
protein
Length
243 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
PHYCOCYANOBILIN:FERREDOXIN oxidoreductase
EC
1.3.7.5
UniProt
Q55891
Ligands
BLA
Pockets
4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APHYCOCYANOBILIN:FERREDOXIN oxidoreductase (EC 1.3.7.5)protein24342% helix, 24% strandQ55891

Ligands and binding sites

  • BLA · Biliverdine IX alpha · ligand · chains A
  • EDO · 1,2-ethanediol · additive · 7 copies · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12420.720.8640BLA
2670.400.8020empty
3550.290.7520empty
4590.280.7413EDO

Compared structures

  • 3F0M · Crystal structure of radical D105N Synechocystis sp. PcyA · the same entry in another collection · chain A against A, TM-score 1.00
  • Q55891 · AlphaFold monomer V2.0 prediction for PHYCOCYANOBILIN:FERREDOXIN oxidoreductase (Q55891) · a predicted model of the same protein · chain A against A, TM-score 0.98

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