8dd7

The Cryo-EM structure of Drosophila Cryptochrome in complex with Timeless

Method: ELECTRON MICROSCOPY Dmax: 136.1 Å Quality: GOOD

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

Methylated-DNA--protein-cysteine methyltransferase,Cryptochrome-1 fusion

Drosophila melanogaster

UniProt E5BBQ0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–181 Chain B; UniProt 5–181 Not recorded FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.30 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.

7 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name E5BBQ0_HUMAN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 38–218; UniProt 1–181 Author chain B; PDBConstruct 1406–1582; UniProt 5–181

Methylated-DNA--protein-cysteine methyltransferase,Cryptochrome-1 fusion

Drosophila melanogaster

UniProt O77059

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–520 Not recorded Protein timeless,Methylated-DNA--protein-cysteine methyltransferase fusion × 1 (P49021,E5BBQ0) FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.30 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.

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

View Construct and Data Evidence
UniProt name CRY1_DROME
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 227–746; UniProt 1–520

Protein timeless,Methylated-DNA--protein-cysteine methyltransferase fusion

Homo sapiens

UniProt P49021

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–1398 Not recorded Methylated-DNA--protein-cysteine methyltransferase,Cryptochrome-1 fusion × 1 (E5BBQ0,O77059) FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.30 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name TIM_DROME
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1398; UniProt 1–1398

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 8dd7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8dd7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8dd7
Deposition date deposition_date2022-06-17
Structure title titleThe Cryo-EM structure of Drosophila Cryptochrome in complex with Timeless
Keywords keywordsFlavoprotein, Nuclear import, Light-sensor, Armadillo-repeat protein, CIRCADIAN CLOCK PROTEIN; CIRCADIAN CLOCK PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.58
Radius of gyration Rg (electron density) rg_electron41.49
Forward intensity I(0) i0316017000.00
Molecular weight molecular_weight147410.0 kDa
Excluded volume excluded_volume185370 ų
Envelope volume envelope_volume248770 ų
Hydration-shell volume shell_volume51698 ų
Envelope diameter envelope_diameter136.8
Shell Rg shell_rg44.65
Envelope Rg envelope_rg41.20
Shape Rg shape_rg41.51
Total Rg total_rg41.60
Total atoms total_atoms10370
Residues n_residues1275
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 dmax136.1
Rg (real space) rg_real41.78
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real3.1600e+08
I(0) uncertainty (real space) i0_real_error5.4130e+06
Rg (reciprocal space) rg_reciprocal41.58
I(0) (reciprocal space) i0_reciprocal315900000.0000
Solution quality estimate total_estimate0.8042
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary35.8
Skewness Skewness skewness0.407
Kurtosis Kurtosis kurtosis-0.621
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha78360000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.840; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.931; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)