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10es

Chloroplast Glutamyl Peptidase WT in open-open conformation

Method: ELECTRON MICROSCOPY Dmax: 152.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Isoform 2 of Probable glutamyl endopeptidase, chloroplastic

Arabidopsis thaliana

UniProt Q8VZF3

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 63–961 Chain B； UniProt 63–961 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE；7 force, 4 seconds, no wait time or drain time Resolution 3.00 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.

Other PDB Difference from Current Entry 10ES Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
10EO Chloroplast Glutamyl Peptidase S781R in closed-closed conformation Deposited 2026-01-15 Different mutation/modification Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 63–961（899 aa）
Chain B 63–961（899 aa）
Mutation：S781R Mutation：S781R No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；7 force, 4 seconds, no wait time or drain time
Resolution 3.20 Å
10EP Chloroplast Glutamyl Peptidase S781R in open-closed conformation Deposited 2026-01-15 Different mutation/modification Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 63–961（899 aa）
Chain B 63–961（899 aa）
Mutation：S781R Mutation：S781R No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；7 force, 4 seconds, no wait time or drain time
Resolution 3.20 Å
10EQ Chloroplast Glutamyl Peptidase WT in open-closed conformation Deposited 2026-01-15 Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 63–961（899 aa）
Chain B 63–961（899 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；7 force, 4 seconds, no wait time or drain time
Resolution 3.30 Å
10ER Chloroplast Glutamyl Peptidase S781R in open-open conformation Deposited 2026-01-15 Different mutation/modification Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 63–961（899 aa）
Chain B 63–961（899 aa）
Mutation：S781R Mutation：S781R No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；7 force, 4 seconds, no wait time or drain time
Resolution 3.20 Å
10ET Chloroplast Glutamyl Peptidase D855N in open-closed conformation Deposited 2026-01-15 Different mutation/modification Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 63–961（899 aa）
Chain B 63–961（899 aa）
Mutation：D855N Mutation：D855N No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；7 force, 4 seconds, no wait time or drain time
Resolution 3.00 Å
10EU Chloroplast Glutamyl Peptidase D855N in open-open conformation Deposited 2026-01-15 Different mutation/modification Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 63–961（899 aa）
Chain B 63–961（899 aa）
Mutation：D855N Mutation：D855N No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；7 force, 4 seconds, no wait time or drain time
Resolution 3.00 Å

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

View Construct and Data Evidence
UniProt name CGEP_ARATH
Isoform Q8VZF3-2
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 9–907； UniProt 63–961 Author chain B； PDBConstruct 9–907； UniProt 63–961

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 10es

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10es
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10es
Deposition date deposition_date2026-01-15
Structure title titleChloroplast Glutamyl Peptidase WT in open-open conformation
Keywords keywordsS9 protease, enzyme, serine protease, alpha-beta-alpha sandwich fold, beta-propeller, PLANT PROTEIN; PLANT PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier45.38 Å
Radius of gyration Rg (electron density) rg_electron45.05 Å
Forward intensity I(0) i0466932000.00
Molecular weight molecular_weight178320.0 kDa
Excluded volume excluded_volume223560 ų
Envelope volume envelope_volume355190 ų
Hydration-shell volume shell_volume66870 ų
Envelope diameter envelope_diameter160.3 Å
Shell Rg shell_rg49.34 Å
Envelope Rg envelope_rg43.35 Å
Shape Rg shape_rg45.02 Å
Total Rg total_rg45.35 Å
Total atoms total_atoms12586
Residues n_residues1594
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax152.7 Å
Rg (real space) rg_real45.42 Å
Rg uncertainty (real space) rg_real_error2.14 Å
I(0) (real space) i0_real4.6690e+08
I(0) uncertainty (real space) i0_real_error1.0430e+07
Rg (reciprocal space) rg_reciprocal45.38 Å
I(0) (reciprocal space) i0_reciprocal466900000.0000
Solution quality estimate total_estimate0.8826
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.0 Å
Skewness Skewness skewness0.336
Kurtosis Kurtosis kurtosis-0.401
Angular range angular_range— – 0.1750 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41450000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.895
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)