› 1rbl

X-ray diffraction
2.2Å resolution

STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301

Released:
DOI: 10.2210/pdb1rbl/pdb
PDB entry 1rbl coloured by chain, front view.
PDB entry 1rbl coloured by chain, side view.
PDB entry 1rbl coloured by chain, top view.
Source organism: Synechococcus elongatus PCC 6301
Primary publication:
Structure determination and refinement of ribulose 1,5-bisphosphate carboxylase/oxygenase from Synechococcus PCC6301.
Newman J, Branden CI, Jones TA
Acta Crystallogr D Biol Crystallogr 49 548-60 (1993)
PMID: 15299492

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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero hexadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133662 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ribulose bisphosphate carboxylase large chain Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 467 amino acids
Theoretical weight: 51.87 KDa
Source organism: Synechococcus elongatus PCC 6301
Expression system: Not provided
UniProt:
  • Canonical: P00880 (Residues: 6-472; Coverage: 99%)
Gene names: cbbL, rbcA, rbcL, syc0130_c
Sequence domains:
Structure domains:
Ribulose bisphosphate carboxylase small subunit Chains: I, J, K, L, M, N, O, P
Molecule details ›
Chains: I, J, K, L, M, N, O, P
Length: 109 amino acids
Theoretical weight: 12.93 KDa
Source organism: Synechococcus elongatus PCC 6301
Expression system: Not provided
UniProt:
  • Canonical: P04716 (Residues: 2-110; Coverage: 98%)
Gene names: cbbS, rbcS, syc0129_c
Sequence domains: Ribulose bisphosphate carboxylase, small chain
Structure domains: Ribulose bisphosphate carboxylase, small subunit

Ligands and Environments

3 bound ligands:
Ligand MG 8 x MG
Ligand CAP 8 x CAP
Ligand FMT 8 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 223.9Å b: 111.9Å c: 199.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 not available
Expression system: Not provided

Quick links

Citations

6 review citations

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

19 mentions without citation

Function, structure, and evolution of the RubisCO-like proteins and their RubisCO homologs.
Tabita et al. (2007)
18 more