1avr

CRYSTAL AND MOLECULAR STRUCTURE OF HUMAN ANNEXIN V AFTER REFINEMENT. IMPLICATIONS FOR STRUCTURE, MEMBRANE BINDING AND ION CHANNEL FORMATION OF THE ANNEXIN FAMILY OF PROTEINS

Method: X-RAY DIFFRACTION Dmax: 78.5 Å Quality: GOOD

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

ANNEXIN V

Homo sapiens

UniProt P08758

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 1–319 Not recorded CA CALCIUM ION × 5 SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 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.

16 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANXA5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–320; UniProt 1–319

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 1avr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1avr
Deposition date deposition_date1991-10-17
Structure title titleCRYSTAL AND MOLECULAR STRUCTURE OF HUMAN ANNEXIN V AFTER REFINEMENT. IMPLICATIONS FOR STRUCTURE, MEMBRANE BINDING AND ION CHANNEL FORMATION OF THE ANNEXIN FAMILY OF PROTEINS
Keywords keywordsCALCIUM/PHOSPHOLIPID BINDING, CALCIUM-PHOSPHOLIPID BINDING complex; CALCIUM/PHOSPHOLIPID BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.48
Radius of gyration Rg (electron density) rg_electron21.51
Forward intensity I(0) i022266900.00
Molecular weight molecular_weight35884.0 kDa
Excluded volume excluded_volume44919 ų
Envelope volume envelope_volume52965 ų
Hydration-shell volume shell_volume21336 ų
Envelope diameter envelope_diameter77.8
Shell Rg shell_rg27.69
Envelope Rg envelope_rg21.66
Shape Rg shape_rg21.49
Total Rg total_rg22.38
Total atoms total_atoms2512
Residues n_residues317
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 dmax78.5
Rg (real space) rg_real22.52
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real2.2270e+07
I(0) uncertainty (real space) i0_real_error2.9460e+05
Rg (reciprocal space) rg_reciprocal22.51
I(0) (reciprocal space) i0_reciprocal22270000.0000
Solution quality estimate total_estimate0.8569
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.0
Skewness Skewness skewness0.455
Kurtosis Kurtosis kurtosis-0.068
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6243000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.728; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.966; Smooth: 0.987

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_idd1avra_
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_id1avrA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1avrA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1avrA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1avrA04
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin

8. Citations (3)

9. Files and Curves (10)