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1arv

;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: 66.7 Å Quality: GOOD

SAXS Profile

SAXS profile for 1arv

P(r) Distribution

P(r) distribution for 1arv

1. Structure Basics

entry_id1arv
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_guinier20.53
rg_electron19.44
i023781400.00
molecular_weight36248.0 kDa
excluded_volume44871 ų
envelope_volume50270 ų
shell_volume21458 ų
envelope_diameter66.7
shell_rg26.13
envelope_rg19.75
shape_rg19.44
total_rg20.30
total_atoms2540
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)

dmax66.7
rg_real20.44
rg_real_error0.31
i0_real2.3780e+07
i0_real_error2.8680e+05
rg_reciprocal20.46
i0_reciprocal23780000.0000
total_estimate0.8879
solution_quality GOOD a GOOD solution
n_peaks1
r_peak_primary26.1
skewness0.248
kurtosis-0.350
angular_range— – 0.3850 −1
current_alpha0.0001
highest_alpha6333000.0000
n_real_points70
gnom_version4.1.3
quality_criteria AN1: 0.000; Oscil: 0.847; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.999

4. Crystallography & Experiment

5. Entities & Polymer Info (6)

6. Citations (3)

7. Files & Curves (10)