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1amy

CRYSTAL AND MOLECULAR STRUCTURE OF BARLEY ALPHA-AMYLASE

Method: X-RAY DIFFRACTION Dmax: 78.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE

Hordeum vulgare

UniProt P04063

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 25–427 Not recorded CA CALCIUM ION × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 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 1AMY Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AVA AMY2/BASI PROTEIN-PROTEIN COMPLEX FROM BARLEY SEED Deposited 1997-09-15 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 25–427（403 aa）
Not recorded CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.7；pH 6.7
Resolution 1.90 Å R-free 0.269
1AVA AMY2/BASI PROTEIN-PROTEIN COMPLEX FROM BARLEY SEED Deposited 1997-09-15 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 25–427（403 aa）
Not recorded CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.7；pH 6.7
Resolution 1.90 Å R-free 0.269
1BG9 BARLEY ALPHA-AMYLASE WITH SUBSTRATE ANALOGUE ACARBOSE Deposited 1998-06-05 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 25–427（403 aa）
Not recorded CA CALCIUM ION × 6 AF1 4,6-dideoxy-4-{[(1S,4S,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.7；pH 6.7
Resolution 2.80 Å R-free 0.249

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

View Construct and Data Evidence
UniProt name AMY2_HORVU
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–403； UniProt 25–427

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 1amy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1amy
Deposition date deposition_date1994-03-10
Structure title titleCRYSTAL AND MOLECULAR STRUCTURE OF BARLEY ALPHA-AMYLASE
Keywords keywordsHYDROLASE (O-GLYCOSYL); HYDROLASE (O-GLYCOSYL)
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_guinier22.87 Å
Radius of gyration Rg (electron density) rg_electron21.81 Å
Forward intensity I(0) i033645400.00
Molecular weight molecular_weight45039.0 kDa
Excluded volume excluded_volume56297 ų
Envelope volume envelope_volume62390 ų
Hydration-shell volume shell_volume24084 ų
Envelope diameter envelope_diameter79.1 Å
Shell Rg shell_rg28.72 Å
Envelope Rg envelope_rg22.06 Å
Shape Rg shape_rg21.76 Å
Total Rg total_rg22.75 Å
Total atoms total_atoms3187
Residues n_residues403
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 dmax78.8 Å
Rg (real space) rg_real22.86 Å
Rg uncertainty (real space) rg_real_error0.53 Å
I(0) (real space) i0_real3.3650e+07
I(0) uncertainty (real space) i0_real_error4.2160e+05
Rg (reciprocal space) rg_reciprocal22.87 Å
I(0) (reciprocal space) i0_reciprocal33650000.0000
Solution quality estimate total_estimate0.8684
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.7 Å
Skewness Skewness skewness0.390
Kurtosis Kurtosis kurtosis-0.178
Angular range angular_range— – 0.3450 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7076000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.769; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.995
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1amya1
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_idd1amya2
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_id1amyA01
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily80 — Glycosidases
Domain ID domain_id1amyA02
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 (3)

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9. Files and Curves (10)