4qsz

X-ray diffraction
2.86Å resolution

Crystal structure of mouse JMJd7 fused with maltose-binding protein

Released:
Entry authors: Liu H, Wang C, Zhang GY

Function and Biology Details

Reaction catalysed:
A [protein]-L-lysine + 2-oxoglutarate + O(2) = a [protein]-(3S)-hydroxy-L-lysine + succinate + CO(2)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-533023 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional peptidase and (3S)-lysyl hydroxylase Jmjd7; Maltose/maltodextrin-binding periplasmic protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 687 amino acids
Theoretical weight: 76.56 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 27-387; Coverage: 98%)
  • Canonical: P0C872 (Residues: 2-316; Coverage: 100%)
Gene names: JW3994, Jmjd7, b4034, malE
Sequence domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21
Unit cell:
a: 48.09Å b: 158.92Å c: 100.01Å
α: 90° β: 94.08° γ: 90°
R-values:
R R work R free
0.195 0.191 0.264
Expression system: Escherichia coli