› 2now

X-ray diffraction
2.2Å resolution

An unusual twin-His arrangement in the pore of ammonia channels is essential for substrate conductance

Released:
DOI: 10.2210/pdb2now/pdb
PDB entry 2now coloured by chain, front view.
PDB entry 2now coloured by chain, side view.
PDB entry 2now coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
An unusual twin-his arrangement in the pore of ammonia channels is essential for substrate conductance.
Javelle A, Lupo D, Zheng L, Li XD, Winkler FK, Merrick M
J Biol Chem 281 39492-8 (2006)
PMID: 17040913

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159623 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ammonium transporter AmtB Chain: A
Molecule details ›
Chain: A
Length: 424 amino acids
Theoretical weight: 44.44 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P69681 (Residues: 23-428; Coverage: 100%)
Gene names: JW0441, amtB, b0451, ybaG
Sequence domains: Ammonium Transporter Family
Structure domains: Ammonium transporter AmtB like domains

Ligands and Environments

3 bound ligands:
Ligand SO4 2 x SO4
Ligand ACT 1 x ACT
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P63
Unit cell:
a: 110.074Å b: 110.074Å c: 84.619Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.163 0.161 0.195
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Nitrogen assimilation in Escherichia coli: putting molecular data into a systems perspective.
van Heeswijk et al. (2013)
9 more

1 mention without citation

Properties of Cavities in Biological Structures-A Survey of the Protein Data Bank.
Chwastyk et al. (2020)