2zrs

Crystal structure of Ca2+-bound form of des3-23ALG-2

Method: X-RAY DIFFRACTION Dmax: 141.4 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 24–191 Chain B; UniProt 24–191 Fragment:UNP residues 24-191 CA CALCIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;50mM MES, 12.5% 2-propanol, 150mM calcium acetate, pH6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.10 Å R-free 0.280
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 24–191 Chain D; UniProt 24–191 Fragment:UNP residues 24-191 CA CALCIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;50mM MES, 12.5% 2-propanol, 150mM calcium acetate, pH6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.10 Å R-free 0.280
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 24–191 Chain F; UniProt 24–191 Fragment:UNP residues 24-191 CA CALCIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;50mM MES, 12.5% 2-propanol, 150mM calcium acetate, pH6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.10 Å R-free 0.280
4 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 24–191 Chain H; UniProt 24–191 Fragment:UNP residues 24-191 CA CALCIUM ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;50mM MES, 12.5% 2-propanol, 150mM calcium acetate, pH6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.10 Å R-free 0.280

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 16 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 1–168; UniProt 24–191 Author chain B; PDBConstruct 1–168; UniProt 24–191 Author chain C; PDBConstruct 1–168; UniProt 24–191 Author chain D; PDBConstruct 1–168; UniProt 24–191 Author chain E; PDBConstruct 1–168; UniProt 24–191 Author chain F; PDBConstruct 1–168; UniProt 24–191 Author chain G; PDBConstruct 1–168; UniProt 24–191 Author chain H; PDBConstruct 1–168; UniProt 24–191

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 2zrs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2zrs
Deposition date deposition_date2008-09-01
Structure title titleCrystal structure of Ca2+-bound form of des3-23ALG-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_guinier45.13
Radius of gyration Rg (electron density) rg_electron44.59
Forward intensity I(0) i0362987000.00
Molecular weight molecular_weight155400.0 kDa
Excluded volume excluded_volume193480 ų
Envelope volume envelope_volume301790 ų
Hydration-shell volume shell_volume56508 ų
Envelope diameter envelope_diameter150.6
Shell Rg shell_rg50.43
Envelope Rg envelope_rg42.43
Shape Rg shape_rg44.60
Total Rg total_rg44.84
Total atoms total_atoms10956
Residues n_residues1309
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 dmax141.4
Rg (real space) rg_real44.98
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real3.6300e+08
I(0) uncertainty (real space) i0_real_error5.8860e+06
Rg (reciprocal space) rg_reciprocal45.13
I(0) (reciprocal space) i0_reciprocal363000000.0000
Solution quality estimate total_estimate0.8841
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary72.7
Skewness Skewness skewness0.083
Kurtosis Kurtosis kurtosis-0.676
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha47050000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.752

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd2zrsa_
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
Domain ID domain_idd2zrsb_
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
Domain ID domain_idd2zrsc_
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
Domain ID domain_idd2zrsd_
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
Domain ID domain_idd2zrse_
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
Domain ID domain_idd2zrsf_
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
Domain ID domain_idd2zrsg_
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
Domain ID domain_idd2zrsh_
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 (8 domains)

Domain ID domain_id2zrsA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2zrsB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2zrsC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2zrsD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2zrsE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2zrsF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2zrsG00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2zrsH00
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)