› 1fwf

X-ray diffraction
2Å resolution

KLEBSIELLA AEROGENES UREASE, C319D VARIANT

Released:
DOI: 10.2210/pdb1fwf/pdb
PDB entry 1fwf coloured by chain, front view.
PDB entry 1fwf coloured by chain, side view.
PDB entry 1fwf coloured by chain, top view.
Source organism: Klebsiella aerogenes
Primary publication:
Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease.
Pearson MA, Michel LO, Hausinger RP, Karplus PA
Biochemistry 36 8164-72 (1997)
PMID: 9201965

Function and Biology Details

Reaction catalysed: 
Urea + H(2)O = CO(2) + 2 NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero nonamer (preferred)
PDBe Complex ID:
PDB-CPX-148349 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Urease subunit gamma Chain: A
Molecule details ›
Chain: A
Length: 100 amino acids
Theoretical weight: 11.1 KDa
Source organism: Klebsiella aerogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: P18316 (Residues: 1-100; Coverage: 100%)
Gene name: ureA
Sequence domains: Urease, gamma subunit
Structure domains: Urease, gamma-like subunit
Urease subunit beta Chain: B
Molecule details ›
Chain: B
Length: 106 amino acids
Theoretical weight: 11.71 KDa
Source organism: Klebsiella aerogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: P18315 (Residues: 1-106; Coverage: 100%)
Gene name: ureB
Sequence domains: Urease beta subunit
Structure domains: Urease, beta subunit
Urease subunit alpha Chain: C
Molecule details ›
Chain: C
Length: 567 amino acids
Theoretical weight: 60.42 KDa
Source organism: Klebsiella aerogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: P18314 (Residues: 1-567; Coverage: 100%)
Gene name: ureC
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NI 2 x NI
1 modified residue:
Ligand KCX 1 x KCX

Experiments and Validation Details

Entry percentile scores
Spacegroup: I213
Unit cell:
a: 170.8Å b: 170.8Å c: 170.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.171 not available
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies.
Gerlt et al. (2001)
12 more

1 mention without citation

Nonredox nickel enzymes.
Maroney et al. (2014)