› 1k9v

X-ray diffraction
2.4Å resolution

Structural evidence for ammonia tunelling across the (beta-alpha)8-barrel of the imidazole glycerol phosphate synthase bienzyme complex

Released:
DOI: 10.2210/pdb1k9v/pdb
PDB entry 1k9v coloured by chain, front view.
PDB entry 1k9v coloured by chain, side view.
PDB entry 1k9v coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex.
Douangamath A, Walker M, Beismann-Driemeyer S, Vega-Fernandez MC, Sterner R, Wilmanns M
Structure 10 185-93 (2002)
PMID: 11839304

Function and Biology Details

Reactions catalysed: 
L-glutamine + H(2)O = L-glutamate + NH(3)
(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-194696 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Imidazole glycerol phosphate synthase subunit HisH Chain: F
Molecule details ›
Chain: F
Length: 201 amino acids
Theoretical weight: 23.13 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0C8 (Residues: 1-201; Coverage: 100%)
Gene names: TM_1038, hisH
Sequence domains:
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand ACY 1 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21212
Unit cell:
a: 126.008Å b: 35.837Å c: 42.507Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 0.278
Expression system: Escherichia coli

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Citations

11 review citations

Protein Allostery and Conformational Dynamics.
Guo et al. (2016)
10 more

5 mentions without citation

Protein-protein docking benchmark version 3.0.
Hwang et al. (2008)
4 more