2h0l

Crystal Structure of a Mutant of Rat Annexin A5

Method: X-RAY DIFFRACTION Dmax: 74.7 Å Quality: GOOD

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

Annexin A5

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–318 Mutation:YES CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;PEG 4000, 300MM SODIUM ACETATA, 100MM TRIS, 3MM SODIUM AZIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K, pH 8.50 Resolution 2.59 Å R-free 0.278

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 2h0l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2h0l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2h0l
Deposition date deposition_date2006-05-15
Structure title titleCrystal Structure of a Mutant of Rat Annexin A5
Keywords keywordsCALCIUM, PHOSPHOLIPID MEMBRANE BINDING PROTEINS, 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_guinier22.29
Radius of gyration Rg (electron density) rg_electron21.30
Forward intensity I(0) i021330800.00
Molecular weight molecular_weight34867.0 kDa
Excluded volume excluded_volume43540 ų
Envelope volume envelope_volume51671 ų
Hydration-shell volume shell_volume20980 ų
Envelope diameter envelope_diameter77.2
Shell Rg shell_rg27.32
Envelope Rg envelope_rg21.46
Shape Rg shape_rg21.31
Total Rg total_rg22.08
Total atoms total_atoms2449
Residues n_residues316
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 dmax74.7
Rg (real space) rg_real22.30
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real2.1330e+07
I(0) uncertainty (real space) i0_real_error2.9050e+05
Rg (reciprocal space) rg_reciprocal22.30
I(0) (reciprocal space) i0_reciprocal21330000.0000
Solution quality estimate total_estimate0.8778
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.422
Kurtosis Kurtosis kurtosis-0.131
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5704000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.808; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2h0la_
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_id2h0lA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id2h0lA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id2h0lA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id2h0lA04
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)