1l0z

THE STRUCTURE OF PORCINE PANCREATIC ELASTASE COMPLEXED WITH XENON AND BROMIDE, CRYOPROTECTED WITH DRY PARAFFIN OIL

Method: X-RAY DIFFRACTION Dmax: 54.7 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

ELASTASE 1

OrganismNot specified

UniProt P00772

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–266 Not recorded NA SODIUM ION × 1 BR BROMIDE ION × 32 XE XENON × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;298 K;10 mM sodium acetate, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.50 Å R-free 0.209

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

126 other PDB entries and 131 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELA1_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–240; UniProt 27–266

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1l0z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1l0z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1l0z
Deposition date deposition_date2002-02-14
Structure title titleTHE STRUCTURE OF PORCINE PANCREATIC ELASTASE COMPLEXED WITH XENON AND BROMIDE, CRYOPROTECTED WITH DRY PARAFFIN OIL
Keywords keywordsXenon, Bromide, PPE, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier18.23
Radius of gyration Rg (electron density) rg_electron16.78
Forward intensity I(0) i020016500.00
Molecular weight molecular_weight28622.0 kDa
Excluded volume excluded_volume32936 ų
Envelope volume envelope_volume36943 ų
Hydration-shell volume shell_volume18059 ų
Envelope diameter envelope_diameter53.9
Shell Rg shell_rg23.31
Envelope Rg envelope_rg16.94
Shape Rg shape_rg16.57
Total Rg total_rg18.08
Total atoms total_atoms1856
Residues n_residues240
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax54.7
Rg (real space) rg_real18.09
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real2.0020e+07
I(0) uncertainty (real space) i0_real_error2.1990e+05
Rg (reciprocal space) rg_reciprocal18.11
I(0) (reciprocal space) i0_reciprocal20020000.0000
Solution quality estimate total_estimate0.9046
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.6
Skewness Skewness skewness0.072
Kurtosis Kurtosis kurtosis-0.491
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2931000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1l0za_
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.2 — Eukaryotic proteases

CATH v4.4 (2 domains)

Domain ID domain_id1l0zA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1l0zA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases

8. Citations (1)

9. Files and Curves (10)