← Back to search
11as

ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE

Method: X-RAY DIFFRACTION Dmax: 88.2 Å Quality: GOOD
▼

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

ASPARAGINE SYNTHETASE

Escherichia coli K12

UniProt P00963

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 1–330 Chain B； UniProt 1–330 Mutation：C51A, C315A ASN ASPARAGINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；PROTEIN CRYSTALLIZED FROM 45% SATURATED AMMONIUM SULFATE, 22 MM ASPARAGINE, 88 MM MGCL2, 10 %(W/V) GLYCEROL 5 MM 2-MERCAPTOETHANOL, 50 MM HEPES, PH7.5 Resolution 2.50 Å R-free 0.253

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 11AS Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
12AS ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE AND AMP Deposited 1997-12-02 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–330（330 aa）
Chain B 1–330（330 aa）
Mutation：C51A, C315A Mutation：C51A, C315A ASN ASPARAGINE × 2 AMP ADENOSINE MONOPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；PROTEIN CRYSTALLIZED FROM 45% SATURATED AMMONIUM SULFATE, 22 MM ASPARAGINE, 88 MM MGCL2, 10 %(W/V) GLYCEROL 5 MM 2-MERCAPTOETHANOL, 50 MM HEPES, PH7.5 THEN SOAKED BY 50MM AMP AND 50 MM ASPARAGINE
Resolution 2.20 Å R-free 0.287

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

View Construct and Data Evidence
UniProt name ASNA_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–330； UniProt 1–330 Author chain B； PDBConstruct 1–330； UniProt 1–330

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 11as

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 11as
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id11as
Deposition date deposition_date1997-12-02
Structure title titleASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE
Keywords keywordsLIGASE, ASPARAGINE SYNTHETASE, NITROGEN FIXATION; LIGASE
Experimental Method methodX-RAY DIFFRACTION
▼

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

Radius of gyration Rg (Guinier) rg_guinier26.84 Å
Radius of gyration Rg (electron density) rg_electron25.72 Å
Forward intensity I(0) i087431100.00
Molecular weight molecular_weight72688.0 kDa
Excluded volume excluded_volume90738 ų
Envelope volume envelope_volume106550 ų
Hydration-shell volume shell_volume34136 ų
Envelope diameter envelope_diameter90.3 Å
Shell Rg shell_rg33.66 Å
Envelope Rg envelope_rg25.65 Å
Shape Rg shape_rg25.73 Å
Total Rg total_rg26.49 Å
Total atoms total_atoms5136
Residues n_residues654
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
▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax88.2 Å
Rg (real space) rg_real26.79 Å
Rg uncertainty (real space) rg_real_error0.55 Å
I(0) (real space) i0_real8.7430e+07
I(0) uncertainty (real space) i0_real_error1.3160e+06
Rg (reciprocal space) rg_reciprocal26.81 Å
I(0) (reciprocal space) i0_reciprocal87430000.0000
Solution quality estimate total_estimate0.8851
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.4 Å
Skewness Skewness skewness0.340
Kurtosis Kurtosis kurtosis-0.303
Angular range angular_range— – 0.2950 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha32460000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.847; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.967
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (3)

▼

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd11asa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.104 — Class II aaRS and biotin synthetases
Superfamily Superfamily superfamilyd.104.1 — Class II aaRS and biotin synthetases
Family Family familyd.104.1.1 — Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain
Domain ID domain_idd11asb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.104 — Class II aaRS and biotin synthetases
Superfamily Superfamily superfamilyd.104.1 — Class II aaRS and biotin synthetases
Family Family familyd.104.1.1 — Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain

CATH v4.4 (2 domains)

Domain ID domain_id11asA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily10 — Bira Bifunctional Protein; Domain 2
Domain ID domain_id11asB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily10 — Bira Bifunctional Protein; Domain 2
▶

8. Citations (3)

▶

9. Files and Curves (10)