6fxt

X-ray diffraction
2.5Å resolution

Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Cocrystal with Fe2+, Mn2+, UDP-Glc

Released:

Function and Biology Details

Reactions catalysed:
L-lysine-[procollagen] + 2-oxoglutarate + O(2) = (2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO(2)
UDP-alpha-D-galactose + [procollagen]-(2S,5R)-5-hydroxy-L-lysine = UDP + [procollagen]-(2S,5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine
UDP-alpha-D-glucose + [procollagen]-(2S,5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine = UDP + [procollagen]-(2S,5R)-5-O-(alpha-D-glucosyl-(1->2)-beta-D-galactosyl)-5-hydroxy-L-lysine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-130034 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 Chain: A
Molecule details ›
Chain: A
Length: 718 amino acids
Theoretical weight: 82.78 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: O60568 (Residues: 25-738; Coverage: 100%)
Gene name: PLOD3
Sequence domains: 2OG-Fe(II) oxygenase superfamily

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-3
Spacegroup: C2221
Unit cell:
a: 97.744Å b: 100.472Å c: 225.394Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.216 0.248
Expression system: Homo sapiens