› 7c5r

X-ray diffraction
2.31Å resolution

Crystal Structure of C150S mutant Glyceraldehyde-3-phosphate dehydrogenase1 from Escherichia coli complexed with BPG at 2.31 Angstrom resolution

Released:
DOI: 10.2210/pdb7c5r/pdb
PDB entry 7c5r coloured by chain, front view.
PDB entry 7c5r coloured by chain, side view.
PDB entry 7c5r coloured by chain, top view.
Source organism: Escherichia coli BL21(DE3)
Primary publication:
Novel Structures of Type 1 Glyceraldehyde-3-phosphate Dehydrogenase from Escherichia coli Provide New Insights into the Mechanism of Generation of 1,3-Bisphosphoglyceric Acid.
Zhang L, Liu M, Bao L, Boström KI, Yao Y, Li J, Gu S, Ji C
OpenAccess logo Biomolecules 11 (2021)
PMID: 34827563

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102947 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyceraldehyde-3-phosphate dehydrogenase Chains: O, P, Q, R
Molecule details ›
Chains: O, P, Q, R
Length: 352 amino acids
Theoretical weight: 37.87 KDa
Source organism: Escherichia coli BL21(DE3)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A140NCK4 (Residues: 1-333; Coverage: 100%)
Gene name: ECBD_2224
Sequence domains:

Ligands and Environments

6 bound ligands:
Ligand NAD 4 x NAD
Ligand DG4 1 x DG4
Ligand PO4 5 x PO4
Ligand EDO 5 x EDO
Ligand CL 8 x CL
Ligand G3H 3 x G3H
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P41212
Unit cell:
a: 89.398Å b: 89.398Å c: 340.821Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.147 0.203
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 mention without citation

Novel Structures of Type 1 Glyceraldehyde-3-phosphate Dehydrogenase from Escherichia coli Provide New Insights into the Mechanism of Generation of 1,3-Bisphosphoglyceric Acid.
Zhang et al. (2021)