7e0j

LHCII-1 in the state transition supercomplex PSI-LHCI-LHCII from the double phosphatase mutant pph1;pbcp of Chlamydomonas reinhardti.

Method: ELECTRON MICROSCOPY Dmax: 103.0 Å Quality: GOOD

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

Chlorophyll a-b binding protein, chloroplastic

OrganismNot specified

UniProt Q93WE0

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain X; UniProt 1–249 Not recorded Chlorophyll a-b binding protein, chloroplastic × 1 (Q93WL4) Chlorophyll a-b binding protein, chloroplastic × 1 (Q93VE0) CHL CHLOROPHYLL B × 17 CLA CHLOROPHYLL A × 24 LUT (3R,3'R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL × 6 XAT (3S,5R,6S,3'S,5'R,6'S)-5,6,5',6'-DIEPOXY-5,6,5',6'- TETRAHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL × 3 NEX (1R,3R)-6-{(3E,5E,7E,9E,11E,13E,15E,17E)-18-[(1S,4R,6R)-4-HYDROXY-2,2,6-TRIMETHYL-7-OXABICYCLO[4.1.0]HEPT-1-YL]-3,7,12,16-TETRAMETHYLOCTADECA-1,3,5,7,9,11,13,15,17-NONAENYLIDENE}-1,5,5-TRIMETHYLCYCLOHEXANE-1,3-DIOL × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 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 Q93WE0_CHLRE
Isoform
PDB entities 1
Chains and sequence ranges Author chain X; PDBConstruct 1–249; UniProt 1–249

Chlorophyll a-b binding protein, chloroplastic

OrganismNot specified

UniProt Q93WL4

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain Y; UniProt 1–257 Not recorded Chlorophyll a-b binding protein, chloroplastic × 1 (Q93WE0) Chlorophyll a-b binding protein, chloroplastic × 1 (Q93VE0) CHL CHLOROPHYLL B × 17 CLA CHLOROPHYLL A × 24 LUT (3R,3'R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL × 6 XAT (3S,5R,6S,3'S,5'R,6'S)-5,6,5',6'-DIEPOXY-5,6,5',6'- TETRAHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL × 3 NEX (1R,3R)-6-{(3E,5E,7E,9E,11E,13E,15E,17E)-18-[(1S,4R,6R)-4-HYDROXY-2,2,6-TRIMETHYL-7-OXABICYCLO[4.1.0]HEPT-1-YL]-3,7,12,16-TETRAMETHYLOCTADECA-1,3,5,7,9,11,13,15,17-NONAENYLIDENE}-1,5,5-TRIMETHYLCYCLOHEXANE-1,3-DIOL × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q93WL4_CHLRE
Isoform
PDB entities 2
Chains and sequence ranges Author chain Y; PDBConstruct 1–257; UniProt 1–257

Chlorophyll a-b binding protein, chloroplastic

OrganismNot specified

UniProt Q93VE0

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain Z; UniProt 1–256 Non-standard monomer:Yes (specific site not provided by mmCIF) Chlorophyll a-b binding protein, chloroplastic × 1 (Q93WE0) Chlorophyll a-b binding protein, chloroplastic × 1 (Q93WL4) CHL CHLOROPHYLL B × 17 CLA CHLOROPHYLL A × 24 LUT (3R,3'R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL × 6 XAT (3S,5R,6S,3'S,5'R,6'S)-5,6,5',6'-DIEPOXY-5,6,5',6'- TETRAHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL × 3 NEX (1R,3R)-6-{(3E,5E,7E,9E,11E,13E,15E,17E)-18-[(1S,4R,6R)-4-HYDROXY-2,2,6-TRIMETHYL-7-OXABICYCLO[4.1.0]HEPT-1-YL]-3,7,12,16-TETRAMETHYLOCTADECA-1,3,5,7,9,11,13,15,17-NONAENYLIDENE}-1,5,5-TRIMETHYLCYCLOHEXANE-1,3-DIOL × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q93VE0_CHLRE
Isoform
PDB entities 3
Chains and sequence ranges Author chain Z; PDBConstruct 1–256; UniProt 1–256

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 7e0j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7e0j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7e0j
Deposition date deposition_date2021-01-28
Structure title titleLHCII-1 in the state transition supercomplex PSI-LHCI-LHCII from the double phosphatase mutant pph1;pbcp of Chlamydomonas reinhardti.
Keywords keywordsSupercomplex, LHCII, state transition, green alga, Chlamydomonas reinhardtii, PHOTOSYNTHESIS; PHOTOSYNTHESIS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.74
Radius of gyration Rg (electron density) rg_electron28.32
Forward intensity I(0) i0116411000.00
Molecular weight molecular_weight113750.0 kDa
Excluded volume excluded_volume153120 ų
Envelope volume envelope_volume168470 ų
Hydration-shell volume shell_volume46465 ų
Envelope diameter envelope_diameter108.0
Shell Rg shell_rg37.85
Envelope Rg envelope_rg28.90
Shape Rg shape_rg28.29
Total Rg total_rg29.53
Total atoms total_atoms8140
Residues n_residues671
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 dmax103.0
Rg (real space) rg_real30.49
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real1.1640e+08
I(0) uncertainty (real space) i0_real_error1.6770e+06
Rg (reciprocal space) rg_reciprocal30.60
I(0) (reciprocal space) i0_reciprocal116400000.0000
Solution quality estimate total_estimate0.8491
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.6
Skewness Skewness skewness0.034
Kurtosis Kurtosis kurtosis-0.292
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9334000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.692; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd7e0jx_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.43 — Chlorophyll a-b binding protein
Superfamily Superfamily superfamilyf.43.1 — Chlorophyll a-b binding protein
Family Family familyf.43.1.1 — Chlorophyll a-b binding protein
Domain ID domain_idd7e0jy_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.43 — Chlorophyll a-b binding protein
Superfamily Superfamily superfamilyf.43.1 — Chlorophyll a-b binding protein
Family Family familyf.43.1.1 — Chlorophyll a-b binding protein
Domain ID domain_idd7e0jz_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.43 — Chlorophyll a-b binding protein
Superfamily Superfamily superfamilyf.43.1 — Chlorophyll a-b binding protein
Family Family familyf.43.1.1 — Chlorophyll a-b binding protein

8. Citations (1)

9. Files and Curves (10)