5k5g

Structure of human islet amyloid polypeptide in complex with an engineered binding protein

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Islet amyloid polypeptide

Homo sapiens

UniProt P10997

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 3 HI18 × 2 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

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_id5k5g
Deposition date deposition_date2016-05-23
Structure title titleStructure of human islet amyloid polypeptide in complex with an engineered binding protein
Keywords keywordshormone, amyloid, type 2 diabetes, beta-hairpin, signaling protein; HORMONE
Experimental Method methodSOLUTION NMR
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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.

5k5g__assembly_1__model_2

Assembly 1 · Model 2 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5k5g__assembly_1__model_2 | I(q)

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

5k5g__assembly_1__model_2 | 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)14.75 Å
Rg (electron density)13.12 Å
Total Rg14.41 Å
Atom count1622
Residues109
Excluded volume14470 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 5k5g__assembly_1__model_1 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 5k5g__assembly_1__model_2 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 5k5g__assembly_1__model_3 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 5k5g__assembly_1__model_4 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 5k5g__assembly_1__model_5 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 5k5g__assembly_1__model_6 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 5k5g__assembly_1__model_7 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 5k5g__assembly_1__model_8 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 5k5g__assembly_1__model_9 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 5k5g__assembly_1__model_10 trimeric (3) 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 (2)

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6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5k5gB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily420 — Immunoglobulin FC, subunit C
Domain ID domain_id5k5gC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily420 — Immunoglobulin FC, subunit C
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7. Citations (1)