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Reduced form of ornithine hydroxylase (pvda) from pseudomonas aeruginosa

Analyse Reduced form of ornithine hydroxylase (pvda) from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3S61
Type
protein
Length
823 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L-ornithine 5-monooxygenase
EC
1.13.12.-
UniProt
Q51548
Ligands
FAD, ORN, NDP
Pockets
7 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AL-ornithine 5-monooxygenase (EC 1.13.12.-)protein41336% helix, 26% strandQ51548
BL-ornithine 5-monooxygenase (EC 1.13.12.-)protein41034% helix, 25% strandQ51548

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
  • ORN · L-ornithine · ligand · 2 copies · chains A, B
  • NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110990.830.8494FAD, ORN, NDP
29370.830.8489FAD, ORN, NDP
31310.530.8124empty
4730.380.7818empty
5950.370.7517empty

Interfaces

1 interface between chains.

  • A–B · 254 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 3S61 · Reduced Form of Ornithine Hydroxylase (PvdA) from Pseudomonas aeruginosa · the same entry in another collection · chain A against A, TM-score 1.00
  • Q51548 · AlphaFold monomer V2.0 prediction for L-ornithine N(5)-monooxygenase (Q51548) · a predicted model of the same protein · chain B against A, TM-score 0.99

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