1a8b

RAT ANNEXIN V COMPLEXED WITH GLYCEROPHOSPHOETHANOLAMINE

Method: X-RAY DIFFRACTION Dmax: 77.4 Å Quality: GOOD

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

ANNEXIN V

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–318 Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 10 GPE L-ALPHA-GLYCEROPHOSPHORYLETHANOLAMINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.1;PROTEIN CRYSTALLIZED FROM AMMONIUM SULFATE, 20MM CACL2, 50MM HEPES, PH 8.2; SOAKED IN 20% PEG, 20MM CACL2, 50MM GPE, PH 7.1 Resolution 1.90 Å

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 2–319; 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 1a8b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a8b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a8b
Deposition date deposition_date1998-03-23
Structure title titleRAT ANNEXIN V COMPLEXED WITH GLYCEROPHOSPHOETHANOLAMINE
Keywords keywordsPHOSPHOLIPID ANALOG, CALCIUM BINDING PROTEIN, MEMBRANE BINDING PROTEIN; CALCIUM BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.77
Radius of gyration Rg (electron density) rg_electron21.88
Forward intensity I(0) i022683700.00
Molecular weight molecular_weight36199.0 kDa
Excluded volume excluded_volume45276 ų
Envelope volume envelope_volume53140 ų
Hydration-shell volume shell_volume21162 ų
Envelope diameter envelope_diameter78.0
Shell Rg shell_rg27.92
Envelope Rg envelope_rg22.05
Shape Rg shape_rg21.85
Total Rg total_rg22.75
Total atoms total_atoms2526
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 dmax77.4
Rg (real space) rg_real22.81
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real2.2680e+07
I(0) uncertainty (real space) i0_real_error3.2110e+05
Rg (reciprocal space) rg_reciprocal22.80
I(0) (reciprocal space) i0_reciprocal22680000.0000
Solution quality estimate total_estimate0.8719
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.8
Skewness Skewness skewness0.449
Kurtosis Kurtosis kurtosis-0.101
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5134000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.787; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1a8ba_
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_id1a8bA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1a8bA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1a8bA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1a8bA04
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)