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Crystal structure of putative protoporphyrinogen oxidase (YP_001813199.1) from exiguobacterium sp. 255-15 at 2.06 a resolution

Analyse Crystal structure of putative protoporphyrinogen oxidase (YP_001813199.1) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3LOV
Type
protein
Length
451 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protoporphyrinogen oxidase
EC
1.3.3.4
UniProt
B1YKJ9
Ligands
FAD
Pockets
1 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtoporphyrinogen oxidase (EC 1.3.3.4)protein45135% helix, 24% strandB1YKJ9

Ligands and binding sites

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

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19900.830.84105FAD

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

  • 3LOV · Crystal structure of Putative protoporphyrinogen oxidase (YP_001813199.1) from… · the same entry in another collection · chain A against A, TM-score 1.00

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