› 1gud

X-ray diffraction
1.71Å resolution

Hinge-bending motion of D-allose binding protein from Escherichia coli: three open conformations

Released:
DOI: 10.2210/pdb1gud/pdb
PDB entry 1gud coloured by chain, front view.
PDB entry 1gud coloured by chain, side view.
PDB entry 1gud coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structure of D-allose binding protein from Escherichia coli bound to D-allose at 1.8 A resolution.
Chaudhuri BN, Ko J, Park C, Jones TA, Mowbray SL
J Mol Biol 286 1519-31 (1999)
PMID: 10064713

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153855 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-allose-binding periplasmic protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 288 amino acids
Theoretical weight: 30.42 KDa
Source organism: Escherichia coli K-12
UniProt:
  • Canonical: P39265 (Residues: 24-311; Coverage: 100%)
Gene names: JW4049, alsB, b4088, yjcX
Sequence domains: Periplasmic binding protein domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand ZN 8 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 60.229Å b: 64.096Å c: 142.113Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.172 0.212

Quick links

Citations

1 review citation

Polyamine transport in bacteria and yeast.
Igarashi et al. (1999)
25 other articles

10 mentions without citation

Coevolutionary signals across protein lineages help capture multiple protein conformations.
Morcos et al. (2013)
9 more