2je1

The crystal Structure of the tumor supressor protein pp32 (Anp32a) :structural insights into the Anp32 family of proteins

Method: X-RAY DIFFRACTION Dmax: 85.3 Å Quality: EXCELLENT

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

ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32 FAMILY MEMBER A

HOMO SAPIENS

UniProt P39687

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 1–149 Fragment:LRR DOMAIN, RESIDUES 1-149 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;pH 5.50 Resolution 2.69 Å R-free 0.303
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–149 Fragment:LRR DOMAIN, RESIDUES 1-149 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;pH 5.50 Resolution 2.69 Å R-free 0.303
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–149 Fragment:LRR DOMAIN, RESIDUES 1-149 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;pH 5.50 Resolution 2.69 Å R-free 0.303
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 1–149 Fragment:LRR DOMAIN, RESIDUES 1-149 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;pH 5.50 Resolution 2.69 Å R-free 0.303

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.

8 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AN32A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–149; UniProt 1–149 Author chain B; PDBConstruct 1–149; UniProt 1–149 Author chain C; PDBConstruct 1–149; UniProt 1–149 Author chain D; PDBConstruct 1–149; UniProt 1–149

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 2je1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2je1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2je1
Deposition date deposition_date2007-01-12
Structure title titleThe crystal Structure of the tumor supressor protein pp32 (Anp32a) :structural insights into the Anp32 family of proteins
Keywords keywordsNUCLEAR PROTEIN, LEUCINE-RICH REPEAT, LRR, LANP, PHAPI, ANP32, PHOSPHORYLATION; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.14
Radius of gyration Rg (electron density) rg_electron27.78
Forward intensity I(0) i075174000.00
Molecular weight molecular_weight67838.0 kDa
Excluded volume excluded_volume85286 ų
Envelope volume envelope_volume111660 ų
Hydration-shell volume shell_volume33399 ų
Envelope diameter envelope_diameter89.7
Shell Rg shell_rg35.28
Envelope Rg envelope_rg27.33
Shape Rg shape_rg27.77
Total Rg total_rg28.63
Total atoms total_atoms4762
Residues n_residues596
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 dmax85.3
Rg (real space) rg_real28.96
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real7.5170e+07
I(0) uncertainty (real space) i0_real_error1.2170e+06
Rg (reciprocal space) rg_reciprocal29.04
I(0) (reciprocal space) i0_reciprocal75180000.0000
Solution quality estimate total_estimate0.9127
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.1
Skewness Skewness skewness-0.009
Kurtosis Kurtosis kurtosis-0.679
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21160000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.960; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id2je1A00
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily10 — Ribonuclease Inhibitor
Domain ID domain_id2je1B00
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily10 — Ribonuclease Inhibitor
Domain ID domain_id2je1C00
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily10 — Ribonuclease Inhibitor
Domain ID domain_id2je1D00
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily10 — Ribonuclease Inhibitor

8. Citations (1)

9. Files and Curves (10)