› 1h5y

X-ray diffraction
2Å resolution

HisF protein from Pyrobaculum aerophilum

Released:
DOI: 10.2210/pdb1h5y/pdb
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Source organism: Pyrobaculum aerophilum
Primary publication:
Structure of HisF, a histidine biosynthetic protein from Pyrobaculum aerophilum.
Banfield MJ, Lott JS, Arcus VL, McCarthy AA, Baker EN
Acta Crystallogr D Biol Crystallogr 57 1518-25 (2001)
PMID: 11679715

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187428 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Imidazole glycerol phosphate synthase subunit HisF Chains: A, B
Molecule details ›
Chains: A, B
Length: 253 amino acids
Theoretical weight: 27.01 KDa
Source organism: Pyrobaculum aerophilum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8ZY16 (Residues: 3-253; Coverage: 99%)
Gene names: PAE0989, hisF
Sequence domains: Histidine biosynthesis protein
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand PO4 4 x PO4
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P61
Unit cell:
a: 105.896Å b: 105.896Å c: 141.828Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.206 0.227
Expression system: Escherichia coli

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Citations

1 citations in other articles

Crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase from Thermoplasma acidophilum in complex with the substrate sn-glycerol 1-phosphate.
Nemoto et al. (2019)

7 mentions without citation

Two-fold repeated (betaalpha)4 half-barrels may provide a molecular tool for dual substrate specificity.
Kuper et al. (2005)
6 more

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