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Unique non-heme hydroxylase in biosynthesis of nucleoside antibiotic pathway uncover mechanism of reaction

Analyse Unique non-heme hydroxylase in biosynthesis of nucleoside antibiotic pathway… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7V4F
Type
protein
Length
334 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-hydroxylase
UniProt
C4NCJ7
Ligands
5KC, FE, CO2
Pockets
2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
B, ABeta-hydroxylaseprotein16714% helix, 35% strandC4NCJ7

Ligands and binding sites

  • 5KC · (2S,3S)-2-azanyl-4-(2-hydroxy-2-oxoethylamino)-3-oxidanyl-butanoic acid · ligand · chains B
  • FE · Fe (III) ion · metal · 4 copies · chains B, A
  • CO2 · Carbon dioxide · ion · chains B
  • SIN · Succinic acid · additive · 2 copies · chains B, 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17220.760.8163SIN, FE
22770.670.83295KC, SIN, CO2, FE

Interfaces

1 interface between chains.

  • B–A · 448 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 7V4F · Unique non-heme hydroxylase in biosynthesis of nucleoside antibiotic pathway uncover… · the same entry in another collection · chain B against B, TM-score 1.00

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