› 4e1o

X-ray diffraction
1.8Å resolution

Human histidine decarboxylase complex with Histidine methyl ester (HME)

Released:
DOI: 10.2210/pdb4e1o/pdb
PDB entry 4e1o coloured by chain, front view.
PDB entry 4e1o coloured by chain, side view.
PDB entry 4e1o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural study reveals that Ser-354 determines substrate specificity on human histidine decarboxylase.
Komori H, Nitta Y, Ueno H, Higuchi Y
J Biol Chem 287 29175-83 (2012)
PMID: 22767596

Function and Biology Details

Reaction catalysed: 
L-histidine = histamine + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148502 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidine decarboxylase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 481 amino acids
Theoretical weight: 54.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P19113 (Residues: 2-477; Coverage: 72%)
Gene name: HDC
Sequence domains: Pyridoxal-dependent decarboxylase conserved domain
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 6 x PLP
1 bound ligand:
Ligand PVH 6 x PVH
1 modified residue:
Ligand CSX 6 x CSX

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2
Unit cell:
a: 215.163Å b: 112.723Å c: 171.393Å
α: 90° β: 110.3° γ: 90°
R-values:
R R work R free
0.163 0.162 0.181
Expression system: Escherichia coli

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Citations

6 review citations

Expanding the repertoire of L-DOPA's actions: A comprehensive review of its functional neurochemistry.
De Deurwaerdère et al. (2017)
5 more

15 mentions without citation

Current Advances on Structure-Function Relationships of Pyridoxal 5'-Phosphate-Dependent Enzymes.
Liang et al. (2019)
14 more