› 1wsr

X-ray diffraction
2Å resolution

Crystal Structure of Human T-protein of Glycine Cleavage System

Released:
DOI: 10.2210/pdb1wsr/pdb
PDB entry 1wsr coloured by chain, front view.
PDB entry 1wsr coloured by chain, side view.
PDB entry 1wsr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human T-protein of glycine cleavage system at 2.0 A resolution and its implication for understanding non-ketotic hyperglycinemia.
Okamura-Ikeda K, Hosaka H, Yoshimura M, Yamashita E, Toma S, Nakagawa A, Fujiwara K, Motokawa Y, Taniguchi H
J Mol Biol 351 1146-59 (2005)
PMID: 16051266

Function and Biology Details

Reaction catalysed: 
[Protein]-S(8)-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155793 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminomethyltransferase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 375 amino acids
Theoretical weight: 40.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P48728 (Residues: 29-403; Coverage: 93%)
Gene names: AMT, GCST
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 11 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P212121
Unit cell:
a: 54.17Å b: 128.52Å c: 136.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.159 0.193
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Compartmentalization of Mammalian folate-mediated one-carbon metabolism.
Tibbetts et al. (2010)
2 more

2 mentions without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)
1 more