9gzs

WT-IAPP cryo-EM structure Type LLU - control reaction

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Islet amyloid polypeptide

OrganismNot specified

UniProt P10997

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 18 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name IAPP_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–37; UniProt 34–70 Author chain B; PDBConstruct 1–37; UniProt 34–70 Author chain C; PDBConstruct 1–37; UniProt 34–70 Author chain D; PDBConstruct 1–37; UniProt 34–70 Author chain E; PDBConstruct 1–37; UniProt 34–70 Author chain F; PDBConstruct 1–37; UniProt 34–70 Author chain G; PDBConstruct 1–37; UniProt 34–70 Author chain H; PDBConstruct 1–37; UniProt 34–70 Author chain I; PDBConstruct 1–37; UniProt 34–70 Author chain J; PDBConstruct 1–37; UniProt 34–70 Author chain K; PDBConstruct 1–37; UniProt 34–70 Author chain L; PDBConstruct 1–37; UniProt 34–70 Author chain M; PDBConstruct 1–37; UniProt 34–70 Author chain N; PDBConstruct 1–37; UniProt 34–70 Author chain O; PDBConstruct 1–37; UniProt 34–70 Author chain P; PDBConstruct 1–37; UniProt 34–70 Author chain Q; PDBConstruct 1–37; UniProt 34–70 Author chain R; PDBConstruct 1–37; UniProt 34–70

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_id9gzs
Deposition date deposition_date2024-10-04
Structure title titleWT-IAPP cryo-EM structure Type LLU - control reaction
Keywords keywordsAmyloid, IAPP, amylin, aggregation, type-2 diabetes, polymorph, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY
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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.

9gzs__assembly_1__model_1

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

Download this curve (.dat)

9gzs__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.

9gzs__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)27.57 Å
Rg (electron density)27.98 Å
Total Rg28.35 Å
Atom count3000
Residues402
Excluded volume51940 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9gzs__assembly_1__model_1 18-meric (18) 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 (1)

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7. Citations (1)