› 6hrg

X-ray diffraction
2.12Å resolution

Structure of Igni18, a novel metallo hydrolase from the hyperthermophilic archaeon Ignicoccus hospitalis KIN4/I

Released:
DOI: 10.2210/pdb6hrg/pdb
PDB entry 6hrg coloured by chain, front view.
PDB entry 6hrg coloured by chain, side view.
PDB entry 6hrg coloured by chain, top view.
Source organism: Ignicoccus hospitalis
Primary publication:
A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family.
Perez-Garcia P, Kobus S, Gertzen CGW, Hoeppner A, Holzscheck N, Strunk CH, Huber H, Jaeger KE, Gohlke H, Kovacic F, Smits SHJ, Streit WR, Chow J
Commun Biol 4 132 (2021)
PMID: 33514861

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108550 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UPF0173 metal-dependent hydrolase Igni_1254 Chain: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 28.71 KDa
Source organism: Ignicoccus hospitalis
Expression system: Komagataella pastoris
UniProt:
  • Canonical: A8ABX8 (Residues: 1-233; Coverage: 100%)
Gene name: Igni_1254
Sequence domains: Beta-lactamase superfamily domain

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand PO4 1 x PO4
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID30B
Spacegroup: R32
Unit cell:
a: 67.42Å b: 67.42Å c: 253.77Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.184 0.249
Expression system: Komagataella pastoris

Quick links

Citations

3 review citations

Origin, Diversity, and Multiple Roles of Enzymes with Metallo-β-Lactamase Fold from Different Organisms.
Diene et al. (2023)
2 more

1 mention without citation

A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family.
Perez-Garcia et al. (2021)