2ie6

Annexin V under 2.0 MPa pressure of xenon

Method: X-RAY DIFFRACTION Dmax: 77.0 Å Quality: GOOD

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

Annexin A5

OrganismNot specified

UniProt P14668

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–318 Not recorded CA CALCIUM ION × 18 SO4 SULFATE ION × 12 XE XENON × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;annexin V 10mg/ml, Tris HCL 20mM, PH 8, NACL 235MM, (NH4)SO4 1.76M, CACL2 12MM, HEPES 100MM, NAN3 3MM, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.83 Å R-free 0.200

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.

17 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANXA5_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–318; UniProt 1–318

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 2ie6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ie6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ie6
Deposition date deposition_date2006-09-18
Structure title titleAnnexin V under 2.0 MPa pressure of xenon
Keywords keywordscalcium binding protein, phospholipid binding protein, membrane binding protein, PROTEIN AND METAL BINDING PROTEIN; PROTEIN AND METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.81
Radius of gyration Rg (electron density) rg_electron21.85
Forward intensity I(0) i023771400.00
Molecular weight molecular_weight36356.0 kDa
Excluded volume excluded_volume45136 ų
Envelope volume envelope_volume53017 ų
Hydration-shell volume shell_volume21141 ų
Envelope diameter envelope_diameter78.3
Shell Rg shell_rg27.92
Envelope Rg envelope_rg22.03
Shape Rg shape_rg21.82
Total Rg total_rg22.73
Total atoms total_atoms2531
Residues n_residues318
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 dmax77.0
Rg (real space) rg_real22.86
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real2.3770e+07
I(0) uncertainty (real space) i0_real_error2.9120e+05
Rg (reciprocal space) rg_reciprocal22.85
I(0) (reciprocal space) i0_reciprocal23770000.0000
Solution quality estimate total_estimate0.8737
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.5
Skewness Skewness skewness0.454
Kurtosis Kurtosis kurtosis-0.118
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4870000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.807; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2ie6a_
Class classa — All alpha proteins
Fold Fold folda.65 — Annexin
Superfamily Superfamily superfamilya.65.1 — Annexin
Family Family familya.65.1.1 — Annexin

CATH v4.4 (4 domains)

Domain ID domain_id2ie6A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id2ie6A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id2ie6A03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id2ie6A04
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin

8. Citations (1)

9. Files and Curves (10)