› 7ljh

X-ray diffraction
2.5Å resolution

Structure of poly(aspartic acid) hydrolase PahZ2 with Zn+2 bound

Released:
DOI: 10.2210/pdb7ljh/pdb
PDB entry 7ljh coloured by chain, front view.
PDB entry 7ljh coloured by chain, side view.
PDB entry 7ljh coloured by chain, top view.
Source organism: Sphingomonas sp. KT-1
Primary publication:
Sphingomonas sp. KT-1 PahZ2 Structure Reveals a Role for Conformational Dynamics in Peptide Bond Hydrolysis.
Brambley CA, Yared TJ, Gonzalez M, Jansch AL, Wallen JR, Weiland MH, Miller JM
J Phys Chem B 125 5722-5739 (2021)
PMID: 34060838

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-181141 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase M20 dimerisation domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 425 amino acids
Theoretical weight: 44.94 KDa
Source organism: Sphingomonas sp. KT-1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q769D3 (Residues: 1-1, 22-425; Coverage: 95%)
Gene name: pahZ2
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 28 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 48.399Å b: 146.174Å c: 197.238Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.213
Expression system: Escherichia coli BL21(DE3)

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Citations

1 mention without citation

Sphingomonas sp. KT-1 PahZ2 Structure Reveals a Role for Conformational Dynamics in Peptide Bond Hydrolysis.
Brambley et al. (2021)