1bc3

RECOMBINANT RAT ANNEXIN V, TRIPLE MUTANT (T72K, S144K, S228K)

Method: X-RAY DIFFRACTION Dmax: 77.3 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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–318 Mutation:T72K, S144K, S228K CA CALCIUM ION × 5 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.2;PROTEIN CRYSTALLIZED FROM AMMONIUM SULFATE, 20MM CACL2, 50MM HEPPS, PH 8.2 Resolution 1.95 Å R-free 0.211

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 1bc3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bc3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bc3
Deposition date deposition_date1998-05-04
Structure title titleRECOMBINANT RAT ANNEXIN V, TRIPLE MUTANT (T72K, S144K, S228K)
Keywords keywordsCALCIUM BINDING PROTEIN, PHOSPHOLIPID MEMBRANE BINDING PROTEIN, CALCIUM-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_guinier22.74
Radius of gyration Rg (electron density) rg_electron21.84
Forward intensity I(0) i022251500.00
Molecular weight molecular_weight35976.0 kDa
Excluded volume excluded_volume45071 ų
Envelope volume envelope_volume52737 ų
Hydration-shell volume shell_volume21032 ų
Envelope diameter envelope_diameter78.5
Shell Rg shell_rg27.90
Envelope Rg envelope_rg22.06
Shape Rg shape_rg21.82
Total Rg total_rg22.69
Total atoms total_atoms2520
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 dmax77.3
Rg (real space) rg_real22.79
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real2.2250e+07
I(0) uncertainty (real space) i0_real_error2.9260e+05
Rg (reciprocal space) rg_reciprocal22.78
I(0) (reciprocal space) i0_reciprocal22250000.0000
Solution quality estimate total_estimate0.8688
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.6
Skewness Skewness skewness0.463
Kurtosis Kurtosis kurtosis-0.080
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5385000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.785; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.962

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_idd1bc3a_
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_id1bc3A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1bc3A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1bc3A03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1bc3A04
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)