2zn8

Crystal structure of Zn2+-bound form of ALG-2

Method: X-RAY DIFFRACTION Dmax: 64.0 Å Quality: GOOD

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

Programmed cell death protein 6

Homo sapiens

UniProt O75340

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 2–191 Not recorded ZN ZINC ION × 8 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;25% 2-methyl-2,4-pentanediol, 100mM Cacodylate, 75mM Zinc acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.70 Å R-free 0.260

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.

9 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PDCD6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–190; UniProt 2–191

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 2zn8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2zn8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2zn8
Deposition date deposition_date2008-04-22
Structure title titleCrystal structure of Zn2+-bound form of ALG-2
Keywords keywordsPENTA-EF-HAND PROTEIN, CALCIUM BINDING PROTEIN, Apoptosis, Calcium, Endoplasmic reticulum, Membrane, Nucleus, Polymorphism; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.39
Radius of gyration Rg (electron density) rg_electron18.28
Forward intensity I(0) i07634900.00
Molecular weight molecular_weight19807.0 kDa
Excluded volume excluded_volume24529 ų
Envelope volume envelope_volume29894 ų
Hydration-shell volume shell_volume14499 ų
Envelope diameter envelope_diameter64.5
Shell Rg shell_rg23.30
Envelope Rg envelope_rg18.44
Shape Rg shape_rg18.25
Total Rg total_rg19.21
Total atoms total_atoms1387
Residues n_residues166
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 dmax64.0
Rg (real space) rg_real19.36
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real7.6350e+06
I(0) uncertainty (real space) i0_real_error1.0300e+05
Rg (reciprocal space) rg_reciprocal19.37
I(0) (reciprocal space) i0_reciprocal7635000.0000
Solution quality estimate total_estimate0.8938
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.7
Skewness Skewness skewness0.240
Kurtosis Kurtosis kurtosis-0.453
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha644700.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2zn8a_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id2zn8A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand

8. Citations (1)

9. Files and Curves (10)