7pqe

Structure of SidJ/CaM bound to SdeA in post-catalysis state

Method: ELECTRON MICROSCOPY Dmax: 122.4 Å Quality: GOOD

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

Ubiquitinating/deubiquitinating enzyme SdeA

Legionella pneumophila

UniProt Q5ZTK4

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 A; UniProt 231–1190 Not recorded Calmodulin-dependent glutamylase SidJ × 1 (Q5ZTK6) Calmodulin × 1 (P0DP24) MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SDEA_LEGPH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 20–979; UniProt 231–1190

Calmodulin-dependent glutamylase SidJ

Legionella pneumophila

UniProt Q5ZTK6

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 C; UniProt 99–873 Mutation:E565A Ubiquitinating/deubiquitinating enzyme SdeA × 1 (Q5ZTK4) Calmodulin × 1 (P0DP24) MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

9 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIDJ_LEGPH
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 19–793; UniProt 99–873

Calmodulin

Homo sapiens

UniProt P0DP24

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 B; UniProt 1–149 Not recorded Ubiquitinating/deubiquitinating enzyme SdeA × 1 (Q5ZTK4) Calmodulin-dependent glutamylase SidJ × 1 (Q5ZTK6) MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

11 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 20–168; UniProt 1–149

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 7pqe

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7pqe
Deposition date deposition_date2021-09-17
Structure title titleStructure of SidJ/CaM bound to SdeA in post-catalysis state
Keywords keywordsGlutamylase, Pseudokinase, phosphoribosyl, ubiquitination, Complex, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.39
Radius of gyration Rg (electron density) rg_electron35.67
Forward intensity I(0) i0351046000.00
Molecular weight molecular_weight152380.0 kDa
Excluded volume excluded_volume191000 ų
Envelope volume envelope_volume249600 ų
Hydration-shell volume shell_volume56970 ų
Envelope diameter envelope_diameter131.3
Shell Rg shell_rg42.76
Envelope Rg envelope_rg36.11
Shape Rg shape_rg35.65
Total Rg total_rg36.20
Total atoms total_atoms10745
Residues n_residues1364
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 dmax122.4
Rg (real space) rg_real36.36
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real3.5100e+08
I(0) uncertainty (real space) i0_real_error5.8620e+06
Rg (reciprocal space) rg_reciprocal36.38
I(0) (reciprocal space) i0_reciprocal351100000.0000
Solution quality estimate total_estimate0.8610
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.7
Skewness Skewness skewness0.369
Kurtosis Kurtosis kurtosis-0.177
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha64800000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.723

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (2)

9. Files and Curves (10)