› 7zyy

Electron Microscopy
2.12Å resolution

Cryo-EM structure of Lactococcus lactis pyruvate carboxylase with acetyl-CoA

Released:
DOI: 10.2210/pdb7zyy/pdb
PDB entry 7zyy coloured by chain, front view.
PDB entry 7zyy coloured by chain, side view.
PDB entry 7zyy coloured by chain, top view.
Source organism: Lactococcus lactis
Primary publication:
CryoEM structural exploration of catalytically active enzyme pyruvate carboxylase.
López-Alonso JP, Lázaro M, Gil-Cartón D, Choi PH, Tong L, Valle M
OpenAccess logo Nat Commun 13 6185 (2022)
PMID: 36261450
Related structures: EMD-15028

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-244202 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate carboxylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 1143 amino acids
Theoretical weight: 127.35 KDa
Source organism: Lactococcus lactis
Expression system: Escherichia coli

Ligands and Environments

6 bound ligands:
Ligand MG 8 x MG
Ligand MN 4 x MN
Ligand ADP 4 x ADP
Ligand ACO 4 x ACO
Ligand PYR 4 x PYR
Ligand BCT 4 x BCT
1 modified residue:
Ligand KCX 4 x KCX

Experiments and Validation Details

Entry percentile scores
Resolution: 2.12Å
Relevant EMDB volumes: EMD-15028
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Current Advances of Atomically Dispersed Metal-Centered Nanozymes for Tumor Diagnosis and Therapy.
Tian et al. (2023)
1 other article

1 mention without citation

CryoEM structural exploration of catalytically active enzyme pyruvate carboxylase.
López-Alonso et al. (2022)