2pvt

Crystal structure of a new isoform of phospholipase A2 from russells viper at 2.1 A resolution

Method: X-RAY DIFFRACTION Dmax: 52.8 Å Quality: GOOD

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

phospholipase A2

OrganismNot specified

UniProt P59071

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 1–117 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;298 K;0.3M Ammonium sulphate, 30% PEG8000, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.10 Å R-free 0.217

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.

52 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PA28_DABRR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–117; UniProt 1–117

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 2pvt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2pvt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2pvt
Deposition date deposition_date2007-05-10
Structure title titleCrystal structure of a new isoform of phospholipase A2 from russells viper at 2.1 A resolution
Keywords keywordsCatalysis, Active site, Isoform, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.19
Radius of gyration Rg (electron density) rg_electron14.46
Forward intensity I(0) i03947470.00
Molecular weight molecular_weight13437.0 kDa
Excluded volume excluded_volume16524 ų
Envelope volume envelope_volume19137 ų
Hydration-shell volume shell_volume11523 ų
Envelope diameter envelope_diameter51.5
Shell Rg shell_rg19.77
Envelope Rg envelope_rg14.82
Shape Rg shape_rg14.44
Total Rg total_rg15.56
Total atoms total_atoms932
Residues n_residues121
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 dmax52.8
Rg (real space) rg_real15.15
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real3.9470e+06
I(0) uncertainty (real space) i0_real_error4.4580e+04
Rg (reciprocal space) rg_reciprocal15.15
I(0) (reciprocal space) i0_reciprocal3947000.0000
Solution quality estimate total_estimate0.8658
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.7
Skewness Skewness skewness0.262
Kurtosis Kurtosis kurtosis-0.376
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1060000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.772; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2pvta_
Class classa — All alpha proteins
Fold Fold folda.133 — Phospholipase A2, PLA2
Superfamily Superfamily superfamilya.133.1 — Phospholipase A2, PLA2
Family Family familya.133.1.2 — Vertebrate phospholipase A2

CATH v4.4 (1 domains)

Domain ID domain_id2pvtA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology90 — Phospholipase A2
Homologous superfamily homologous superfamily10 — Phospholipase A2 domain

8. Citations (1)

9. Files and Curves (10)