1xjl

Structure of human annexin A2 in the presence of calcium ions

Method: X-RAY DIFFRACTION Dmax: 101.9 Å Quality: GOOD

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

Annexin A2

Homo sapiens

UniProt P07355

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 20–338 Chain B; UniProt 20–338 Mutation:A66E CA CALCIUM ION × 14 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;PEG8000, calcium acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.59 Å R-free 0.264

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.

40 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANXA2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–319; UniProt 20–338 Author chain B; PDBConstruct 1–319; UniProt 20–338

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 1xjl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1xjl
Deposition date deposition_date2004-09-23
Structure title titleStructure of human annexin A2 in the presence of calcium ions
Keywords keywordsannexins, calcium-binding protein, lipid-binding protein, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.35
Radius of gyration Rg (electron density) rg_electron32.18
Forward intensity I(0) i085399300.00
Molecular weight molecular_weight73530.0 kDa
Excluded volume excluded_volume92156 ų
Envelope volume envelope_volume119410 ų
Hydration-shell volume shell_volume32172 ų
Envelope diameter envelope_diameter110.4
Shell Rg shell_rg37.64
Envelope Rg envelope_rg31.72
Shape Rg shape_rg32.17
Total Rg total_rg32.68
Total atoms total_atoms5138
Residues n_residues638
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 dmax101.9
Rg (real space) rg_real32.52
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real8.5400e+07
I(0) uncertainty (real space) i0_real_error1.3140e+06
Rg (reciprocal space) rg_reciprocal32.46
I(0) (reciprocal space) i0_reciprocal85390000.0000
Solution quality estimate total_estimate0.8153
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary99.8
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis-0.636
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13330000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.902; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.908; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1xjla_
Class classa — All alpha proteins
Fold Fold folda.65 — Annexin
Superfamily Superfamily superfamilya.65.1 — Annexin
Family Family familya.65.1.1 — Annexin
Domain ID domain_idd1xjlb_
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 (8 domains)

Domain ID domain_id1xjlA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1xjlA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1xjlA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1xjlA04
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1xjlB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1xjlB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1xjlB03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily10 — Annexin
Domain ID domain_id1xjlB04
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)