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1c5i

;HYDROGEN BONDING AND CATALYSIS: AN UNEXPECTED EXPLANATION FOR HOW A SINGLE AMINO ACID SUBSTITUTION CAN CHANGE THE PH OPTIMUM OF A GLYCOSIDASE ;

Method: X-RAY DIFFRACTION Dmax: 48.2 Å Quality: EXCELLENT

SAXS Profile

SAXS profile for 1c5i

P(r) Distribution

P(r) distribution for 1c5i

1. Structure Basics

entry_id1c5i
deposition_date1999-11-24
title;HYDROGEN BONDING AND CATALYSIS: AN UNEXPECTED EXPLANATION FOR HOW A SINGLE AMINO ACID SUBSTITUTION CAN CHANGE THE PH OPTIMUM OF A GLYCOSIDASE ;
keywordsGLYCOSIDASE, PH-DEPENDENT ENZYME MECHANISM, GENERAL ACID/ BASE CATALYSIS, ISOTOPE SHIFT, SHORT HYDROGEN BONDS, XYLAN, HYDROLASE; HYDROLASE
methodX-RAY DIFFRACTION

Download Data

2. SAXS Parameters (CRYSOL)

rg_guinier16.25
rg_electron14.87
i08429990.00
molecular_weight20667.0 kDa
excluded_volume25422 ų
envelope_volume27014 ų
shell_volume14980 ų
envelope_diameter47.0
shell_rg21.20
envelope_rg15.07
shape_rg14.83
total_rg16.01
total_atoms1466
n_residues185
n_harmonics20
q_range— – 0.5000 −1
n_points101
shell_typedirectional
solvent_density0.3340 e/ų
contrast_shell0.0300 e/ų
crysol_version4.1.3

3. P(r) Analysis (GNOM)

dmax48.2
rg_real16.08
rg_real_error0.19
i0_real8.4300e+06
i0_real_error8.5480e+04
rg_reciprocal16.10
i0_reciprocal8430000.0000
total_estimate0.9036
solution_quality EXCELLENT a EXCELLENT solution
n_peaks2
r_peak_primary22.2
skewness-0.006
kurtosis-0.532
angular_range— – 0.4900 −1
current_alpha0.0000
highest_alpha2564000.0000
n_real_points79
gnom_version4.1.3
quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.997

4. Crystallography & Experiment

5. Entities & Polymer Info (3)

6. Citations (1)

7. Files & Curves (10)