› 1hpc

X-ray diffraction
2Å resolution

REFINED STRUCTURES AT 2 ANGSTROMS AND 2.2 ANGSTROMS OF THE TWO FORMS OF THE H-PROTEIN, A LIPOAMIDE-CONTAINING PROTEIN OF THE GLYCINE DECARBOXYLASE

Released:
DOI: 10.2210/pdb1hpc/pdb
PDB entry 1hpc coloured by chain, front view.
PDB entry 1hpc coloured by chain, side view.
PDB entry 1hpc coloured by chain, top view.
Source organism: Pisum sativum
Primary publication:
Refined structures at 2 and 2.2 A resolution of two forms of the H-protein, a lipoamide-containing protein of the glycine decarboxylase complex.
Pares S, Cohen-Addad C, Sieker LC, Neuburger M, Douce R
Acta Crystallogr D Biol Crystallogr 51 1041-51 (1995)
PMID: 15299773

Function and Biology Details

Reaction catalysed: 
Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L-lysine + CO(2)
Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147590 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycine cleavage system H protein, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 131 amino acids
Theoretical weight: 13.96 KDa
Source organism: Pisum sativum
Expression system: Not provided
UniProt:
  • Canonical: P16048 (Residues: 35-165; Coverage: 79%)
Gene names: GCDH, GDCSH
Sequence domains: Glycine cleavage H-protein
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments


Cofactor: Ligand LPB 1 x LPB

Cofactor: Ligand LPA 1 x LPA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 57.3Å b: 57.3Å c: 136.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.185 not available
Expression system: Not provided

Quick links

Citations

4 citation in other articles

Crystal structure of a component of glycine cleavage system: T-protein from Pyrococcus horikoshii OT3 at 1.5 A resolution.
Lokanath et al. (2005)
3 more

4 mentions without citation

Enzymatic Conversion of CO2: From Natural to Artificial Utilization.
Bierbaumer et al. (2023)
3 more