› 7cdh

X-ray diffraction
2.6Å resolution

Crystal structure of Betaaspartyl dipeptidase from thermophilic keratin degrading Fervidobacterium islandicum-AW-1

Released:
DOI: 10.2210/pdb7cdh/pdb
PDB entry 7cdh coloured by chain, front view.
PDB entry 7cdh coloured by chain, side view.
PDB entry 7cdh coloured by chain, top view.
Source organism: Fervidobacterium islandicum
Primary publication:
Functional Characterization of Primordial Protein Repair Enzyme M38 Metallo-Peptidase From Fervidobacterium islandicum AW-1.
La JW, Dhanasingh I, Jang H, Lee SH, Lee DW
Front Mol Biosci 7 600634 (2020)
PMID: 33392259

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-103238 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isoaspartyl dipeptidase Chain: X
Molecule details ›
Chain: X
Length: 387 amino acids
Theoretical weight: 42.41 KDa
Source organism: Fervidobacterium islandicum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A1B0VPV0 (Residues: 1-387; Coverage: 100%)
Gene names: NA23_08080, iadA
Sequence domains: Amidohydrolase family

Ligands and Environments

3 bound ligands:
Ligand GOL 7 x GOL
Ligand PEG 2 x PEG
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: I422
Unit cell:
a: 143.94Å b: 143.94Å c: 119.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.163 0.223
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Thermo-L-Asparaginases: From the Role in the Viability of Thermophiles and Hyperthermophiles at High Temperatures to a Molecular Understanding of Their Thermoactivity and Thermostability.
Dumina et al. (2023)

1 mention without citation

Functional Characterization of Primordial Protein Repair Enzyme M38 Metallo-Peptidase From Fervidobacterium islandicum AW-1.
La et al. (2020)