1g5n

ANNEXIN V COMPLEX WITH HEPARIN OLIGOSACCHARIDES

Method: X-RAY DIFFRACTION Dmax: 78.2 Å Quality: GOOD

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

ANNEXIN V

Rattus norvegicus

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 Other combination Monomer Protein × 1 其他Polymer 2 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–318 Not recorded ;4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose ; × 2 CA CALCIUM ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:soaking;pH 8.2;290 K;PEG 4000, calcium chloride, HEPES buffer, pH 8.2, soaking, temperature 290.0K Resolution 1.90 Å R-free 0.238

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 ANX5_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 1g5n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1g5n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1g5n
Deposition date deposition_date2000-11-01
Structure title titleANNEXIN V COMPLEX WITH HEPARIN OLIGOSACCHARIDES
Keywords keywordshelix-bundle, membrane binding, heparin, heparan sulfate, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.35
Radius of gyration Rg (electron density) rg_electron22.19
Forward intensity I(0) i027302000.00
Molecular weight molecular_weight38277.0 kDa
Excluded volume excluded_volume47177 ų
Envelope volume envelope_volume56000 ų
Hydration-shell volume shell_volume21950 ų
Envelope diameter envelope_diameter79.6
Shell Rg shell_rg28.34
Envelope Rg envelope_rg22.33
Shape Rg shape_rg22.12
Total Rg total_rg23.15
Total atoms total_atoms2653
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 dmax78.2
Rg (real space) rg_real23.40
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real2.7300e+07
I(0) uncertainty (real space) i0_real_error3.4760e+05
Rg (reciprocal space) rg_reciprocal23.39
I(0) (reciprocal space) i0_reciprocal27300000.0000
Solution quality estimate total_estimate0.8744
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.9
Skewness Skewness skewness0.458
Kurtosis Kurtosis kurtosis-0.079
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5369000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.800; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.986

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_idd1g5na_
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_id1g5nA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1g5nA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1g5nA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1g5nA04
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)