8io2

The Rubisco assembly intermidate of Arabidopsis thaliana Rubisco accumulation factor 1 (AtRaf1) and Rubisco large subunit (RbcL)

Method: ELECTRON MICROSCOPY Dmax: 191.2 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ribulose bisphosphate carboxylase large chain

Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)

UniProt P00880

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain A; UniProt 2–472 Chain B; UniProt 2–472 Chain C; UniProt 2–472 Chain D; UniProt 2–472 Chain E; UniProt 2–472 Chain F; UniProt 2–472 Chain G; UniProt 2–472 Chain H; UniProt 2–472 Not recorded Rubisco accumulation factor 1.2, chloroplastic × 9 (Q9SR19) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBL_SYNP6
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–471; UniProt 2–472 Author chain B; PDBConstruct 1–471; UniProt 2–472 Author chain C; PDBConstruct 1–471; UniProt 2–472 Author chain D; PDBConstruct 1–471; UniProt 2–472 Author chain E; PDBConstruct 1–471; UniProt 2–472 Author chain F; PDBConstruct 1–471; UniProt 2–472 Author chain G; PDBConstruct 1–471; UniProt 2–472 Author chain H; PDBConstruct 1–471; UniProt 2–472

Rubisco accumulation factor 1.2, chloroplastic

Arabidopsis thaliana

UniProt Q9SR19

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain I; UniProt 73–437 Chain J; UniProt 73–437 Chain K; UniProt 73–437 Chain L; UniProt 73–437 Chain M; UniProt 73–437 Chain N; UniProt 73–437 Chain O; UniProt 73–437 Chain P; UniProt 73–437 Chain Q; UniProt 73–437 Not recorded Ribulose bisphosphate carboxylase large chain × 8 (P00880) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

6 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAF2_ARATH
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–346; UniProt 73–437 Author chain J; PDBConstruct 1–346; UniProt 73–437 Author chain K; PDBConstruct 1–346; UniProt 73–437 Author chain L; PDBConstruct 1–346; UniProt 73–437 Author chain M; PDBConstruct 1–346; UniProt 73–437 Author chain N; PDBConstruct 1–346; UniProt 73–437 Author chain O; PDBConstruct 1–346; UniProt 73–437 Author chain P; PDBConstruct 1–346; UniProt 73–437 Author chain Q; PDBConstruct 1–346; UniProt 73–437

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8io2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8io2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8io2
Deposition date deposition_date2023-03-10
Structure title titleThe Rubisco assembly intermidate of Arabidopsis thaliana Rubisco accumulation factor 1 (AtRaf1) and Rubisco large subunit (RbcL)
Keywords keywordsRubisco assembly intermediate, CHAPERONE, LYASE; LYASE
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier57.66
Radius of gyration Rg (electron density) rg_electron57.99
Forward intensity I(0) i03754790000.00
Molecular weight molecular_weight519280.0 kDa
Excluded volume excluded_volume651240 ų
Envelope volume envelope_volume936460 ų
Hydration-shell volume shell_volume130770 ų
Envelope diameter envelope_diameter216.8
Shell Rg shell_rg62.25
Envelope Rg envelope_rg58.76
Shape Rg shape_rg57.99
Total Rg total_rg58.10
Total atoms total_atoms36624
Residues n_residues4721
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax191.2
Rg (real space) rg_real57.64
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real3.7550e+09
I(0) uncertainty (real space) i0_real_error6.8250e+07
Rg (reciprocal space) rg_reciprocal57.65
I(0) (reciprocal space) i0_reciprocal3755000000.0000
Solution quality estimate total_estimate0.8756
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary70.8
Skewness Skewness skewness0.401
Kurtosis Kurtosis kurtosis-0.080
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha324900000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.846; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.846

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)