SAXSdb — 3g7v

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

Maltose-binding periplasmic protein, Islet amyloid polypeptide fusion protein

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 2 其他Polymer 2	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 SULFATE ION × 7 GLYCEROL × 3 water × 2	Consistent with protein count
2	Insufficient information	Homooligomer	Protein 2 其他Polymer 2	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 SULFATE ION × 8 GLYCEROL × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MALE_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–367； UniProt 27–392 Author chain B； PDBConstruct 2–367； UniProt 27–392 Author chain C； PDBConstruct 2–367； UniProt 27–392 Author chain D； PDBConstruct 2–367； UniProt 27–392

Maltose-binding periplasmic protein, Islet amyloid polypeptide fusion protein

Homo sapiens

UniProt P10997

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 2 其他Polymer 2	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 SULFATE ION × 7 GLYCEROL × 3 water × 2	Consistent with protein count
2	Insufficient information	Homooligomer	Protein 2 其他Polymer 2	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 SULFATE ION × 8 GLYCEROL × 2 water × 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 372–407； UniProt 34–69 Author chain B； PDBConstruct 372–407； UniProt 34–69 Author chain C； PDBConstruct 372–407； UniProt 34–69 Author chain D； PDBConstruct 372–407； UniProt 34–69

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_id	3g7v
Deposition date deposition_date	2009-02-10
Structure title title	Islet Amyloid Polypeptide (IAPP or Amylin) fused to Maltose Binding Protein
Keywords keywords	;native fold for amyloidogenic protein, Sugar transport, Transport, Amidation, Amyloid, Cleavage on pair of basic residues, Hormone, Secreted, SUGAR BINDING PROTEIN ;; Sugar binding protein, Hormone
Experimental Method method	X-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.

3g7v__assembly_1__model_1

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

Download this curve (.dat)

3g7v__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3g7v__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	31.82 Å
Rg (electron density)	31.17 Å
Total Rg	31.91 Å
Atom count	6233
Residues	798
Excluded volume	111190 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3g7v__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3g7v__assembly_2__model_1`	dimeric （2）	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)

Entity 1 Entity 1 polymer

Description description	Maltose-binding periplasmic protein, Islet amyloid polypeptide fusion protein
Molecular weight formula_weight	44442.2 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	13356

MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALAAAQTNAAAKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY

Source Source

Source organism organism	Homo sapiens
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 branched

Description description	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose
Molecular weight formula_weight	342.3 kDa
Source method src_method	man
Copy count entity_count	4

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	15

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	862

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6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id	3g7vA02
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	2190 —

Domain ID domain_id	3g7vB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	3g7vC00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	3g7vD01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	3g7vD02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	3g7vD03
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	2190 —

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Unit-cell length a length_a	104.025 Å
Unit-cell length b length_b	96.407 Å
Unit-cell length c length_c	103.996 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.53 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.860 Å
Low-resolution limit resolution_low	73.920 Å
R factor r_factor	0.1780
R_work r_work	0.1760
R_free r_free	0.2050

Islet Amyloid Polypeptide (IAPP or Amylin) fused to Maltose Binding Protein

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

Maltose-binding periplasmic protein, Islet amyloid polypeptide fusion protein

State in the Current Structure

Other States of the Same Protein in the Database

Maltose-binding periplasmic protein, Islet amyloid polypeptide fusion protein

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3g7v__assembly_1__model_1

3g7v__assembly_1__model_1 | I(q)

3g7v__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 branched

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (1)

Islet Amyloid Polypeptide (IAPP or Amylin) fused to Maltose Binding Protein

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

Maltose-binding periplasmic protein, Islet amyloid polypeptide fusion protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Maltose-binding periplasmic protein, Islet amyloid polypeptide fusion protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3g7v__assembly_1__model_1

3g7v__assembly_1__model_1 | I(q)

3g7v__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 branched

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (1)