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1c5h

;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: 48.1 Å Quality: EXCELLENT

SAXS Profile

SAXS profile for 1c5h

P(r) Distribution

P(r) distribution for 1c5h

1. Structure Basics

entry_id1c5h
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 ;
keywords;GLYCOSIDASE, PH-DEPENDENT ENZYME MECHANISM, GENERAL ACID/ BASE CATALYSIS, X-RAY CYRSTALLOGRAPHY, ISOTOPE SHIFT, SHORT HYDROGEN BONDS, XYLAN, HYDROLASE ;; HYDROLASE
methodX-RAY DIFFRACTION

Download Data

2. SAXS Parameters (CRYSOL)

rg_guinier16.31
rg_electron14.93
i08271110.00
molecular_weight20398.0 kDa
excluded_volume25088 ų
envelope_volume27058 ų
shell_volume14993 ų
envelope_diameter46.6
shell_rg21.22
envelope_rg15.08
shape_rg14.89
total_rg16.09
total_atoms1448
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)

dmax48.1
rg_real16.15
rg_real_error0.19
i0_real8.2710e+06
i0_real_error7.6000e+04
rg_reciprocal16.16
i0_reciprocal8271000.0000
total_estimate0.9043
solution_quality EXCELLENT a EXCELLENT solution
n_peaks2
r_peak_primary22.2
skewness-0.013
kurtosis-0.538
angular_range— – 0.4900 −1
current_alpha0.0000
highest_alpha2359000.0000
n_real_points79
gnom_version4.1.3
quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.994

4. Crystallography & Experiment

5. Entities & Polymer Info (2)

6. Citations (1)

7. Files & Curves (10)