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1arx

;CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS ;

Method: X-RAY DIFFRACTION Dmax: 65.3 Å Quality: GOOD

SAXS Profile

SAXS profile for 1arx

P(r) Distribution

P(r) distribution for 1arx

1. Structure Basics

entry_id1arx
deposition_date1995-04-25
title;CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS ;
keywordsPEROXIDASE (DONOR:H2O2 OXIDOREDUCTASE); PEROXIDASE (DONOR:H2O2 OXIDOREDUCTASE)
methodX-RAY DIFFRACTION

Download Data

2. SAXS Parameters (CRYSOL)

rg_guinier20.24
rg_electron19.37
i026543100.00
molecular_weight37150.0 kDa
excluded_volume45167 ų
envelope_volume50583 ų
shell_volume21557 ų
envelope_diameter67.0
shell_rg26.13
envelope_rg19.78
shape_rg19.45
total_rg19.99
total_atoms2546
n_residues336
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)

dmax65.3
rg_real20.16
rg_real_error0.36
i0_real2.6540e+07
i0_real_error3.0500e+05
rg_reciprocal20.18
i0_reciprocal26540000.0000
total_estimate0.8844
solution_quality GOOD a GOOD solution
n_peaks2
r_peak_primary25.2
skewness0.270
kurtosis-0.288
angular_range— – 0.3950 −1
current_alpha0.0000
highest_alpha3934000.0000
n_real_points71
gnom_version4.1.3
quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.954

4. Crystallography & Experiment

5. Entities & Polymer Info (7)

6. Citations (3)

7. Files & Curves (10)