› 1urp

X-ray diffraction
2.3Å resolution

D-RIBOSE-BINDING PROTEIN FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1urp/pdb
PDB entry 1urp coloured by chain, front view.
PDB entry 1urp coloured by chain, side view.
PDB entry 1urp coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Multiple open forms of ribose-binding protein trace the path of its conformational change.
Björkman AJ, Mowbray SL
J Mol Biol 279 651-64 (1998)
PMID: 9641984

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-136386 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribose import binding protein RbsB Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 271 amino acids
Theoretical weight: 28.51 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P02925 (Residues: 26-296; Coverage: 100%)
Gene names: JW3730, b3751, prlB, rbsB, rbsP
Sequence domains: Periplasmic binding protein domain
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 60.099Å b: 120.954Å c: 64.131Å
α: 90° β: 90.05° γ: 90°
R-values:
R R work R free
0.235 0.235 0.267
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Structure, function, and evolution of bacterial ATP-binding cassette systems.
Davidson et al. (2008)
2 more

40 mentions without citation

Integrated Modeling Program, Applied Chemical Theory (IMPACT).
Banks et al. (2005)
39 more