› 1gk2

X-ray diffraction
1.9Å resolution

Histidine Ammonia-Lyase (HAL) Mutant F329G from Pseudomonas putida

Released:
DOI: 10.2210/pdb1gk2/pdb
PDB entry 1gk2 coloured by chain, front view.
PDB entry 1gk2 coloured by chain, side view.
PDB entry 1gk2 coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Autocatalytic peptide cyclization during chain folding of histidine ammonia-lyase.
Baedeker M, Schulz GE
Structure 10 61-7 (2002)
PMID: 11796111

Function and Biology Details

Reaction catalysed: 
L-histidine = urocanate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149201 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidine ammonia-lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 509 amino acids
Theoretical weight: 53.57 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P21310 (Residues: 2-510; Coverage: 100%)
Gene name: hutH
Sequence domains: Aromatic amino acid lyase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 4 x GOL
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUB200
Spacegroup: P21
Unit cell:
a: 77.966Å b: 130.561Å c: 115.835Å
α: 90° β: 91° γ: 90°
R-values:
R R work R free
0.17 not available 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Protein posttranslational modifications: the chemistry of proteome diversifications.
Walsh et al. (2005)
5 more

1 mention without citation

Structural and functional roles of coevolved sites in proteins.
Chakrabarti et al. (2010)