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7eqx

Crystal structure of an Aedes aegypti procarboxypeptidase B1

Method: X-RAY DIFFRACTION Dmax: 103.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Carboxypeptidase B

Aedes aegypti

UniProt Q6J661

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 19–113 Chain C； UniProt 114–412 Fragment：Pro-region Fragment：Mature region ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；0.2M Ammonium sulphate, 0.1M sodium cacodylate trihydrate pH 6.5, 30% w/v PEG 8000 Resolution 2.08 Å R-free 0.198
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain B； UniProt 19–113 Chain D； UniProt 114–412 Fragment：Pro-region Fragment：Mature region ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；0.2M Ammonium sulphate, 0.1M sodium cacodylate trihydrate pH 6.5, 30% w/v PEG 8000 Resolution 2.08 Å R-free 0.198

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 7EQX Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7EQZ Crystal structure of Carboxypeptidase B complexed with Potato Carboxypeptidase Inhibitor Deposited 2021-05-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 114–412（299 aa） Fragment：Mature region
Not recorded ZN ZINC ION × 1 GLY GLYCINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；1.6M Ammonium sulfate, 0.1M Sodium HEPES pH 7.5, 0.1M Sodium chloride
Resolution 2.20 Å R-free 0.196

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6J661_AEDAE
Isoform —
PDB entities 1, 2
Chains and sequence ranges Author chain A； PDBConstruct 4–98； UniProt 19–113 Author chain B； PDBConstruct 4–98； UniProt 19–113 Author chain C； PDBConstruct 1–299； UniProt 114–412 Author chain D； PDBConstruct 1–299； UniProt 114–412

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 7eqx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7eqx
Deposition date deposition_date2021-05-05
Structure title titleCrystal structure of an Aedes aegypti procarboxypeptidase B1
Keywords keywordsProcarboxypeptidase B1, ANTIVIRAL PROTEIN, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier30.46 Å
Radius of gyration Rg (electron density) rg_electron30.46 Å
Forward intensity I(0) i0111944000.00
Molecular weight molecular_weight83618.0 kDa
Excluded volume excluded_volume104230 ų
Envelope volume envelope_volume124190 ų
Hydration-shell volume shell_volume35191 ų
Envelope diameter envelope_diameter103.1 Å
Shell Rg shell_rg36.26 Å
Envelope Rg envelope_rg30.37 Å
Shape Rg shape_rg30.44 Å
Total Rg total_rg31.03 Å
Total atoms total_atoms5904
Residues n_residues757
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 dmax103.5 Å
Rg (real space) rg_real30.65 Å
Rg uncertainty (real space) rg_real_error0.88 Å
I(0) (real space) i0_real1.1190e+08
I(0) uncertainty (real space) i0_real_error1.7700e+06
Rg (reciprocal space) rg_reciprocal30.57 Å
I(0) (reciprocal space) i0_reciprocal111900000.0000
Solution quality estimate total_estimate0.8402
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.9 Å
Skewness Skewness skewness0.525
Kurtosis Kurtosis kurtosis-0.297
Angular range angular_range— – 0.2600 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha74950000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.730; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.874; Smooth: 0.853
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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8. Citations (1)

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9. Files and Curves (10)