1y38

Crystal structure of the complex formed between phospholipase A2 dimer and glycerophosphate at 2.4 A resolution

Method: X-RAY DIFFRACTION Dmax: 59.9 Å Quality: GOOD

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

Phospholipase A2 VRV-PL-VIIIa

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–121 Chain B; UniProt 1–121 Not recorded NA SODIUM ION × 1 SO4 SULFATE ION × 1 G3P SN-GLYCEROL-3-PHOSPHATE × 2 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;25mM Cacodylate, 0.3M ammonium sulphate, 30% PEG 8000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.44 Å R-free 0.224

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_DABRP
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–121; UniProt 1–121 Author chain B; PDBConstruct 1–121; UniProt 1–121

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 1y38

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1y38
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1y38
Deposition date deposition_date2004-11-24
Structure title titleCrystal structure of the complex formed between phospholipase A2 dimer and glycerophosphate at 2.4 A resolution
Keywords keywordscatalysis, inhibition, complex, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.01
Radius of gyration Rg (electron density) rg_electron18.39
Forward intensity I(0) i015225300.00
Molecular weight molecular_weight27843.0 kDa
Excluded volume excluded_volume34220 ų
Envelope volume envelope_volume40674 ų
Hydration-shell volume shell_volume18570 ų
Envelope diameter envelope_diameter62.5
Shell Rg shell_rg24.50
Envelope Rg envelope_rg18.49
Shape Rg shape_rg18.38
Total Rg total_rg19.31
Total atoms total_atoms1924
Residues n_residues242
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 dmax59.9
Rg (real space) rg_real18.91
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real1.5230e+07
I(0) uncertainty (real space) i0_real_error1.9160e+05
Rg (reciprocal space) rg_reciprocal18.92
I(0) (reciprocal space) i0_reciprocal15230000.0000
Solution quality estimate total_estimate0.7562
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.8
Skewness Skewness skewness0.152
Kurtosis Kurtosis kurtosis-0.452
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6769000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.902; Stabil: 1.000; Sysdev: 0.374; Positv: 1.000; Valcen: 1.000; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1y38a_
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
Domain ID domain_idd1y38b_
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 (2 domains)

Domain ID domain_id1y38A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology90 — Phospholipase A2
Homologous superfamily homologous superfamily10 — Phospholipase A2 domain
Domain ID domain_id1y38B00
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)