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7aew

14-3-3 sigma bound to bis-phosphorylated aminopeptidase N (APN, CD13) via canonical and non-canonical binding motifs

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

14-3-3 protein sigma

Homo sapiens

UniProt P31947

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 6 Aminopeptidase N × 4 （P15144） SODIUM ION × 8 CHLORIDE ION × 2 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

Monomer

None

Homodimer
1yz5 3t0l 3t0m 3u9x 4dhm 4dhn 4dho 4dhp 4dhq 4dhr 4dhs 4dht

21 assemblies; showing the first 12

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex
1ywt 1ywt 3iqj 3iqu 3iqv 3lw1 3mhr 3o8i 3p1n 3p1o 3p1p 3p1q

523 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name 1433S_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain AAA； PDBConstruct 6–236； UniProt 1–231

Aminopeptidase N

OrganismNot specified

UniProt P15144

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 6 14-3-3 protein sigma × 2 （P31947） SODIUM ION × 8 CHLORIDE ION × 2 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

Monomer

None

Homodimer

None

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex
4fyq 4fyr 4fys 4fyt 5lhd 5lhd 5lhd 5lhd 6atk 6atk 6atk 6u7e

24 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name AMPN_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain BBB； PDBConstruct 1–38； UniProt 36–73 Author chain CCC； PDBConstruct 1–38； UniProt 36–73

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id7aew
Deposition date deposition_date2020-09-18
Structure title title14-3-3 sigma bound to bis-phosphorylated aminopeptidase N (APN, CD13) via canonical and non-canonical binding motifs
Keywords keywordsextracellular 14-3-3, phosphorylation, aminopeptidase N, CD13, protein binding, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

7aew__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

7aew__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

7aew__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）27.43 Å
Rg (electron density)26.51 Å
Total Rg27.30 Å
Atom count7724
Residues496
Excluded volume69188 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 7aew__assembly_1__model_1 hexameric （6） Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

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7. Citations (1)