› 6yyv

X-ray diffraction
1.77Å resolution

Aspartyl/Asparaginyl beta-hydroxylase (AspH) oxygenase and TPR domains in complex with manganese and 3-methyl-2-oxoglutarate

Released:
DOI: 10.2210/pdb6yyv/pdb
PDB 6yyv coloured by chain and viewed from the front.
PDB 6yyv coloured by chain and viewed from the side.
PDB 6yyv coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Synthesis of 2-oxoglutarate derivatives and their evaluation as cosubstrates and inhibitors of human aspartate/asparagine-beta-hydroxylase
Brewitz L, Nakashima Y, Schofield CJ
Chem Sci 12 1327-1342 (2021)

Function and Biology Details

Reaction catalysed: 
Peptide L-aspartate + 2-oxoglutarate + O(2) = peptide 3-hydroxy-L-aspartate + succinate + CO(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartyl/asparaginyl beta-hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 429 amino acids
Theoretical weight: 49.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12797 (Residues: 330-758; Coverage: 57%)
Gene names: ASPH, BAH
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand MN 1 x MN
Ligand Q1Z 1 x Q1Z
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 48.802Å b: 70.521Å c: 174.488Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.208
Expression system: Escherichia coli BL21(DE3)

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