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1jae

STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE

Method: X-RAY DIFFRACTION Dmax: 78.2 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ALPHA-AMYLASE

OrganismNot specified

UniProt P56634

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 2–471 Fragment：RESIDUES 1 - 471 Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；200 MM SODIUM ACETATE, 100 MM BISTRIS-HCL PH 6.5 30% W/V PEG 8000 Resolution 1.65 Å R-free 0.206

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 1JAE Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CLV YELLOW MEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE AMARANTH ALPHA-AMYLASE INHIBITOR Deposited 1999-05-04 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 2–471（470 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.4；12% PEG 1000, 12% PEG 8000, pH 5.4
Resolution 2.00 Å R-free 0.190
1TMQ STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR Deposited 1998-01-13 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 2–471（470 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions 200MM AMMONIUM PHOSPHATE, 100MM TRIS-HCL, PH 8.5, 50% (W/V) 2-METHYL-2,4- PENTANEDIOL
Resolution 2.50 Å R-free 0.261
1VIW TENEBRIO MOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX Deposited 1998-07-21 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 2–471（470 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7
Resolution 3.00 Å R-free 0.291
1VIW TENEBRIO MOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX Deposited 1998-07-21 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 2–471（470 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7
Resolution 3.00 Å R-free 0.291

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AMY_TENMO
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–471； UniProt 2–471

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 1jae

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1jae
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1jae
Deposition date deposition_date1997-09-30
Structure title titleSTRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE
Keywords keywordsGLYCOSIDASE, ALPHA-AMYLASE, CARBOHYDRATE METABOLISM, ALPHA-1, 4-GLUCAN-4-GLUCANOHYDROLASE, HYDROLASE; GLYCOSIDASE
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_guinier23.50 Å
Radius of gyration Rg (electron density) rg_electron22.22 Å
Forward intensity I(0) i048617900.00
Molecular weight molecular_weight51271.0 kDa
Excluded volume excluded_volume62696 ų
Envelope volume envelope_volume70170 ų
Hydration-shell volume shell_volume26266 ų
Envelope diameter envelope_diameter80.1 Å
Shell Rg shell_rg29.41 Å
Envelope Rg envelope_rg22.37 Å
Shape Rg shape_rg22.20 Å
Total Rg total_rg23.02 Å
Total atoms total_atoms3608
Residues n_residues470
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 dmax78.2 Å
Rg (real space) rg_real23.45 Å
Rg uncertainty (real space) rg_real_error0.51 Å
I(0) (real space) i0_real4.8620e+07
I(0) uncertainty (real space) i0_real_error6.8790e+05
Rg (reciprocal space) rg_reciprocal23.46 Å
I(0) (reciprocal space) i0_reciprocal48620000.0000
Solution quality estimate total_estimate0.6754
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.7 Å
Skewness Skewness skewness0.335
Kurtosis Kurtosis kurtosis-0.233
Angular range angular_range— – 0.3400 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8370000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.818; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.999; Smooth: 0.976
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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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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1jaea1
Class classb — All beta proteins
Fold Fold foldb.71 — Glycosyl hydrolase domain
Superfamily Superfamily superfamilyb.71.1 — Glycosyl hydrolase domain
Family Family familyb.71.1.1 — alpha-Amylases, C-terminal beta-sheet domain
Domain ID domain_idd1jaea2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.8 — (Trans)glycosidases
Family Family familyc.1.8.1 — Amylase, catalytic domain

CATH v4.4 (2 domains)

Domain ID domain_id1jaeA01
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily80 — Glycosidases
Domain ID domain_id1jaeA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1180 — Golgi alpha-mannosidase II
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8. Citations (2)

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9. Files and Curves (10)