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1ele

;STRUCTURAL ANALYSIS OF THE ACTIVE SITE OF PORCINE PANCREATIC ELASTASE BASED ON THE X-RAY CRYSTAL STRUCTURES OF COMPLEXES WITH TRIFLUOROACETYL-DIPEPTIDE-ANILIDE INHIBITORS ;

Method: X-RAY DIFFRACTION D_max: 54.3 Å Quality: REASONABLE

SAXS Profile

P(r) Distribution

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1. Structure Basics

entry_id	1ele
deposition_date	1994-10-24
title	;STRUCTURAL ANALYSIS OF THE ACTIVE SITE OF PORCINE PANCREATIC ELASTASE BASED ON THE X-RAY CRYSTAL STRUCTURES OF COMPLEXES WITH TRIFLUOROACETYL-DIPEPTIDE-ANILIDE INHIBITORS ;
keywords	HYDROLASE-HYDROLASE INHIBITOR COMPLEX, SERINE PROTEINASE; HYDROLASE/HYDROLASE INHIBITOR
method	X-RAY DIFFRACTION

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Download Data

SAXS curve (.dat) P(r) distribution (.pr.out) Structure (CIF)

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2. SAXS Parameters (CRYSOL)

rg_guinier	17.67 Å
rg_electron	16.64 Å
i0	24534600.00
molecular_weight	24671.0 kDa
excluded_volume	23468 Å³
envelope_volume	36671 Å³
shell_volume	17962 Å³
envelope_diameter	55.0 Å
shell_rg	23.23 Å
envelope_rg	16.93 Å
shape_rg	16.62 Å
total_rg	17.39 Å
total_atoms	1857
n_residues	240
n_harmonics	20
q_range	— – 0.5000 Å⁻¹
n_points	101
shell_type	directional
solvent_density	0.3340 e/Å³
contrast_shell	0.0300 e/Å³
crysol_version	4.1.3

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3. P(r) Analysis (GNOM)

dmax	54.3 Å
rg_real	17.53 Å
rg_real_error	0.19 Å
i0_real	2.4530e+07
i0_real_error	2.3900e+05
rg_reciprocal	17.54 Å
i0_reciprocal	24530000.0000
total_estimate	0.7361
solution_quality	REASONABLE a REASONABLE solution
n_peaks	2
r_peak_primary	22.4 Å
skewness	0.124
kurtosis	-0.460
angular_range	— – 0.4500 Å⁻¹
current_alpha	0.0000
highest_alpha	5891000.0000
n_real_points	76
gnom_version	4.1.3
quality_criteria	AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 0.291; Positv: 1.000; Valcen: 0.988; Smooth: 0.984

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4. Crystallography & Experiment

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5. Entities & Polymer Info (5)

Entity 1 polymer

description	ELASTASE
formula_weight	25928.0 kDa
ec_number	3.4.21.36
src_method	man
entity_count	1

Polymer

type	polypeptide(L)
strand_id	E
atom_count	2001

VVGGTEAQRNSWPSQISLQYRSGSSWAHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNNGTEQYVGVQKIVVHPYWNTDDVAAGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAICSSSSYWGSTVKNSMVCAGGDGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSRLGCNVTRKPTVFTRVSAYISWINNVIASN

Source

organism	Sus scrofa
common_name	pig
ncbi_taxonomy_id	9823

Entity 2 non-polymer

description	N-(trifluoroacetyl)-L-valyl-N-[4-(trifluoromethyl)phenyl]-L-alaninamide
formula_weight	427.3 kDa
src_method	syn
entity_count	1

Entity 3 non-polymer

description	CALCIUM ION
formula_weight	40.1 kDa
src_method	syn
entity_count	1

Entity 4 non-polymer

description	SULFATE ION
formula_weight	96.1 kDa
src_method	syn
entity_count	1

Entity 5 water

description	water
formula_weight	18.0 kDa
src_method	nat
entity_count	137

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6. Citations (8)

;Structural analysis of the active site of porcine pancreatic elastase based on the X-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors. ;

Biochemistry (1995)

PMID: 7880814 · DOI: 10.1021/bi00010a008 PRIMARY

Analogous Inhibitors of Elastase Do not Always Bind Analogously

Nat.Struct.Biol. (1994)

Interaction of the Peptide Cf3-Leu-Ala-Nh-C6H4-Cf3(Tfla) with Porcine Pancreatic Elastase. X-Ray Studies at 1.8 Angstroms

J.Mol.Recog. (1990)

Structure of Native Porcine Pancreatic Elastase at 1.65 Angstroms Resolution

Acta Crystallogr.,Sect.B (1988)

Structure of the Product Complex of Acetyl-Ala-Pro-Ala with Porcine Pancreatic Elastase at 1.65 Angstroms Resolution

J.Mol.Biol. (1986)

Crystallographic Study of the Binding of a Tri-Fluoroacetyl Dipeptide Anilide Inhibitor with Elastase

J.Mol.Biol. (1982)

The Indirect Mechanism of Action of the Trifluoroacetyl Peptides on Elastase

Eur.J.Biochem. (1980)

;The Atomic Structure of Crystalline Porcine Pancreatic Elastase at 2.5 Angstroms Resolution. Comparisons with the Structure of Alpha-Chymotrypsin ;

J.Mol.Biol. (1978)

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length_a	52.400 Å
length_b	57.600 Å
length_c	75.300 Å
angle_alpha	90.00 °
angle_beta	90.00 °
angle_gamma	90.00 °
z_pdb	4

space_group	P 21 21 21
int_tables_number	19
crystal_system	—

resolution	2.000 Å
resolution_low	10.000 Å
r_factor	0.1710
r_work	0.1710
r_free	—

fit	/app/data/saxs_computation/el/1ele/1ele.fit
pddf	/app/data/pr_computation/el/1ele/1ele.pr.out
profile	/app/data/saxs_computation/el/1ele/1ele.dat