› 1rba

X-ray diffraction
2.6Å resolution

SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE RESULTS IN CONFORMATIONAL CHANGES

Released:
DOI: 10.2210/pdb1rba/pdb
PDB entry 1rba coloured by chain, front view.
PDB entry 1rba coloured by chain, side view.
PDB entry 1rba coloured by chain, top view.
Source organism: Rhodospirillum rubrum
Primary publication:
Substitution of ASP193 to ASN at the active site of ribulose-1,5-bisphosphate carboxylase results in conformational changes.
Söderlind E, Schneider G, Gutteridge S
Eur J Biochem 206 729-35 (1992)
PMID: 1606957

Function and Biology Details

Reaction catalysed: 
2 3-phospho-D-glycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO(2) + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138159 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribulose bisphosphate carboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 466 amino acids
Theoretical weight: 50.54 KDa
Source organism: Rhodospirillum rubrum
Expression system: Not provided
UniProt:
  • Canonical: P04718 (Residues: 1-466; Coverage: 100%)
Gene names: cbbL2, cbbM, rbpL
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 65.5Å b: 69.3Å c: 103.1Å
α: 90° β: 92.1° γ: 90°
R-values:
R R work R free
0.207 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Structure and function of Rubisco.
Andersson et al. (2008)
3 more