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1hoe

CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A

Method: X-RAY DIFFRACTION Dmax: 40.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ALPHA-AMYLASE INHIBITOR

Streptomyces tendae

UniProt P01092

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 31–104 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 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 1HOE Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BVN PIG PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE PROTEINACEOUS INHIBITOR TENDAMISTAT Deposited 1998-09-16 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain T 31–104（74 aa）
Not recorded CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；PROTEIN: 12 MG/ML IN 50 MM TRIS/HCL, PH 8.0, MIXED 5:1 WITH 40% (W/V) PEG 1000; RESERVOIR: 0.18-0.20 M SODIUM PHOSPHATE, PH 8.0 HARVESTED IN: 3 M SODIUM ACETATE, PH 7.5
Resolution 2.50 Å R-free 0.260
1OK0 Crystal Structure of Tendamistat Deposited 2003-07-16 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 31–104（74 aa）
Not recorded GOL GLYCEROL × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 1.5；20MG OF LYOPHILIZED PROTEIN WERE DISSOLVED IN 1ML OF DOUBLE-DISTILLED WATER. USING THE HANGING DROP METHOD WITH DROPS OF 2MUL PROTEIN SOLUTION (20 MG/ML) AND 2MUL RESERVOIR SOLUTION (0.1-0.5 M NACL ADJUSTED TO PH 1.3 WITH HYDROCHLORIC ACID), YIELDED TUFT-SHAPED AGGLOMERATES OF ESSENTIALLY ONE-DIMENSIONAL CRYSTALS. STREAK SEEDING {EM VIA} A CAT WHISKER AFTER TOUCHING THESE AGGLOMERATES GAVE SINGLE CRYSTALS WITH DIMENSIONS UP TO 0.1 X 0.01 X 0.01MM^3
Resolution 0.93 Å R-free 0.130
2AIT DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF THE ALPHA-AMYLASE INHIBITOR TENDAMISTAT IN AQUEOUS SOLUTION BY NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY Deposited 1989-05-24 Different experimental method Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 31–104（74 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
3AIT RESTRAINED ENERGY REFINEMENT WITH TWO DIFFERENT ALGORITHMS AND FORCE FIELDS OF THE STRUCTURE OF THE ALPHA-AMYLASE INHIBITOR TENDAMISTAT DETERMINED BY NMR IN SOLUTION Deposited 1990-05-14 Different experimental method Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 31–104（74 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
4AIT RESTRAINED ENERGY REFINEMENT WITH TWO DIFFERENT ALGORITHMS AND FORCE FIELDS OF THE STRUCTURE OF THE ALPHA-AMYLASE INHIBITOR TENDAMISTAT DETERMINED BY NMR IN SOLUTION Deposited 1990-05-14 Different experimental method Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 31–104（74 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IAA_STRTE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–74； UniProt 31–104

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 1hoe

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1hoe
Deposition date deposition_date1989-01-27
Structure title titleCRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A
Keywords keywordsGLYCOSIDASE INHIBITOR; GLYCOSIDASE INHIBITOR
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_guinier12.75 Å
Radius of gyration Rg (electron density) rg_electron11.63 Å
Forward intensity I(0) i01535140.00
Molecular weight molecular_weight7957.0 kDa
Excluded volume excluded_volume9741 ų
Envelope volume envelope_volume10743 ų
Hydration-shell volume shell_volume8265 ų
Envelope diameter envelope_diameter38.7 Å
Shell Rg shell_rg16.70 Å
Envelope Rg envelope_rg11.86 Å
Shape Rg shape_rg11.61 Å
Total Rg total_rg12.89 Å
Total atoms total_atoms558
Residues n_residues74
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 dmax40.8 Å
Rg (real space) rg_real12.69 Å
Rg uncertainty (real space) rg_real_error0.24 Å
I(0) (real space) i0_real1.5350e+06
I(0) uncertainty (real space) i0_real_error1.6150e+04
Rg (reciprocal space) rg_reciprocal12.70 Å
I(0) (reciprocal space) i0_reciprocal1535000.0000
Solution quality estimate total_estimate0.8984
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.5 Å
Skewness Skewness skewness0.171
Kurtosis Kurtosis kurtosis-0.447
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha249500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.929
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1hoea_
Class classb — All beta proteins
Fold Fold foldb.5 — alpha-Amylase inhibitor tendamistat
Superfamily Superfamily superfamilyb.5.1 — alpha-Amylase inhibitor tendamistat
Family Family familyb.5.1.1 — alpha-Amylase inhibitor tendamistat

CATH v4.4 (1 domains)

Domain ID domain_id1hoeA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily20 — Alpha-amylase inhibitor
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8. Citations (1)

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9. Files and Curves (10)