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1cpu

;SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT ;

Method: X-RAY DIFFRACTION Dmax: 85.4 Å Quality: GOOD

SAXS Profile

SAXS profile for 1cpu

P(r) Distribution

P(r) distribution for 1cpu
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1. Structure Basics

entry_id1cpu
deposition_date1999-06-07
title;SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT ;
keywordsAMYLASE, ACARBOSE, GLYCOSYLATION, MUTAGENESIS, DIABETES, CATALYSIS, PANCREATIC, ENZYME, HUMAN, HYDROLASE; HYDROLASE
methodX-RAY DIFFRACTION
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Download Data

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2. SAXS Parameters (CRYSOL)

rg_guinier24.00 Å
rg_electron22.94 Å
i055864800.00
molecular_weight56943.0 kDa
excluded_volume70466 ų
envelope_volume78329 ų
shell_volume28226 ų
envelope_diameter83.2 Å
shell_rg30.53 Å
envelope_rg23.12 Å
shape_rg22.93 Å
total_rg23.76 Å
total_atoms4016
n_residues495
n_harmonics20
q_range— – 0.5000 Å−1
n_points101
shell_typedirectional
solvent_density0.3340 e/ų
contrast_shell0.0300 e/ų
crysol_version4.1.3
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3. P(r) Analysis (GNOM)

dmax85.4 Å
rg_real23.94 Å
rg_real_error0.59 Å
i0_real5.5860e+07
i0_real_error7.3340e+05
rg_reciprocal23.95 Å
i0_reciprocal55870000.0000
total_estimate0.8473
solution_quality GOOD a GOOD solution
n_peaks1
r_peak_primary29.4 Å
skewness0.347
kurtosis-0.197
angular_range— – 0.3300 Å−1
current_alpha0.0000
highest_alpha11660000.0000
n_real_points65
gnom_version4.1.3
quality_criteria AN1: 0.000; Oscil: 0.679; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 1.000
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4. Crystallography & Experiment

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5. Entities & Polymer Info (8)

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6. Citations (1)

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7. Files & Curves (10)