› 6jc8

X-ray diffraction
2.25Å resolution

Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with amino donor L-Glu

Released:
DOI: 10.2210/pdb6jc8/pdb
PDB entry 6jc8 coloured by chain, front view.
PDB entry 6jc8 coloured by chain, side view.
PDB entry 6jc8 coloured by chain, top view.
Source organism: Actinoalloteichus sp. WH1-2216-6
Primary publication:
Structural studies reveal flexible roof of active site responsible for ω-transaminase CrmG overcoming by-product inhibition.
Xu J, Tang X, Zhu Y, Yu Z, Su K, Zhang Y, Dong Y, Zhu W, Zhang C, Wu R, Liu J
Commun Biol 3 455 (2020)
PMID: 32814814

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124895 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CrmG Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 523 amino acids
Theoretical weight: 57.22 KDa
Source organism: Actinoalloteichus sp. WH1-2216-6
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: H8Y6N2 (Residues: 1-523; Coverage: 100%)
Sequence domains: Aminotransferase class-III

Ligands and Environments

2 bound ligands:
Ligand PL6 4 x PL6
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P1
Unit cell:
a: 84.09Å b: 83.93Å c: 88.459Å
α: 106.6° β: 109.11° γ: 95.13°
R-values:
R R work R free
0.179 0.177 0.215
Expression system: Escherichia coli BL21(DE3)

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Citations

2 citation in other articles

Kinetic Characterization and Catalytic Mechanism of N-Acetylornithine Aminotransferase Encoded by slr1022 Gene from Synechocystis sp. PCC6803.
Li et al. (2023)
1 more

1 mention without citation

Structural studies reveal flexible roof of active site responsible for ω-transaminase CrmG overcoming by-product inhibition.
Xu et al. (2020)