4asr

Crystal structure of ANCE in complex with Thr6-Bradykinin

Method: X-RAY DIFFRACTION Dmax: 85.6 Å Quality: GOOD

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

ANGIOTENSIN-CONVERTING ENZYME

DROSOPHILA MELANOGASTER

UniProt Q10714

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 17–614 Fragment:RESIDUES 17-614 BRADYKININ × 1 (P01042) ;beta-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ZN ZINC ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 FLC CITRATE ANION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;100 MM HEPES 1.3 M SODIUM CITRATE, pH 7.5 Resolution 1.90 Å R-free 0.200

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.

26 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACE_DROME
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–598; UniProt 17–614

BRADYKININ

OrganismNot specified

UniProt P01042

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain P; UniProt 381–389 Mutation:YES ANGIOTENSIN-CONVERTING ENZYME × 1 (Q10714) ;beta-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ZN ZINC ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 FLC CITRATE ANION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;100 MM HEPES 1.3 M SODIUM CITRATE, pH 7.5 Resolution 1.90 Å R-free 0.200

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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KNG1_HUMA
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–9; UniProt 381–389

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 4asr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4asr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4asr
Deposition date deposition_date2012-05-02
Structure title titleCrystal structure of ANCE in complex with Thr6-Bradykinin
Keywords keywordsHYDROLASE, ZINC METALLOPROTEASE, SUBSTRATE RECOGNITION; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.55
Radius of gyration Rg (electron density) rg_electron24.43
Forward intensity I(0) i081597600.00
Molecular weight molecular_weight71116.0 kDa
Excluded volume excluded_volume88917 ų
Envelope volume envelope_volume105240 ų
Hydration-shell volume shell_volume34548 ų
Envelope diameter envelope_diameter86.8
Shell Rg shell_rg32.95
Envelope Rg envelope_rg24.81
Shape Rg shape_rg24.39
Total Rg total_rg25.46
Total atoms total_atoms5017
Residues n_residues602
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 dmax85.6
Rg (real space) rg_real25.43
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real8.1600e+07
I(0) uncertainty (real space) i0_real_error1.2400e+06
Rg (reciprocal space) rg_reciprocal25.46
I(0) (reciprocal space) i0_reciprocal81600000.0000
Solution quality estimate total_estimate0.8699
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.8
Skewness Skewness skewness0.238
Kurtosis Kurtosis kurtosis-0.263
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21270000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.771; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)