SAXSdb — 9ivp

▼

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

DARPin,Ferritin heavy chain, N-terminally processed

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 48	Maltodextrin-binding protein × 24 （C3SHQ8）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FRIH_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 193–350； UniProt 20–177 Author chain BA； PDBConstruct 193–350； UniProt 20–177 Author chain C； PDBConstruct 193–350； UniProt 20–177 Author chain DA； PDBConstruct 193–350； UniProt 20–177 Author chain E； PDBConstruct 193–350； UniProt 20–177 Author chain FA； PDBConstruct 193–350； UniProt 20–177 Author chain G； PDBConstruct 193–350； UniProt 20–177 Author chain HA； PDBConstruct 193–350； UniProt 20–177 Author chain I； PDBConstruct 193–350； UniProt 20–177 Author chain JA； PDBConstruct 193–350； UniProt 20–177 Author chain K； PDBConstruct 193–350； UniProt 20–177 Author chain LA； PDBConstruct 193–350； UniProt 20–177 Author chain M； PDBConstruct 193–350； UniProt 20–177 Author chain NA； PDBConstruct 193–350； UniProt 20–177 Author chain O； PDBConstruct 193–350； UniProt 20–177 Author chain PA； PDBConstruct 193–350； UniProt 20–177 Author chain Q； PDBConstruct 193–350； UniProt 20–177 Author chain RA； PDBConstruct 193–350； UniProt 20–177 Author chain S； PDBConstruct 193–350； UniProt 20–177 Author chain TA； PDBConstruct 193–350； UniProt 20–177 Author chain V； PDBConstruct 193–350； UniProt 20–177 Author chain VA； PDBConstruct 193–350； UniProt 20–177 Author chain X； PDBConstruct 193–350； UniProt 20–177 Author chain Z； PDBConstruct 193–350； UniProt 20–177

Maltodextrin-binding protein

Escherichia coli

UniProt C3SHQ8

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 48	DARPin,Ferritin heavy chain, N-terminally processed × 24 （P02794）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	C3SHQ8_ECOLX
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain AA； PDBConstruct 22–387； UniProt 27–392 Author chain B； PDBConstruct 22–387； UniProt 27–392 Author chain CA； PDBConstruct 22–387； UniProt 27–392 Author chain D； PDBConstruct 22–387； UniProt 27–392 Author chain EA； PDBConstruct 22–387； UniProt 27–392 Author chain F； PDBConstruct 22–387； UniProt 27–392 Author chain GA； PDBConstruct 22–387； UniProt 27–392 Author chain H； PDBConstruct 22–387； UniProt 27–392 Author chain IA； PDBConstruct 22–387； UniProt 27–392 Author chain J； PDBConstruct 22–387； UniProt 27–392 Author chain KA； PDBConstruct 22–387； UniProt 27–392 Author chain L； PDBConstruct 22–387； UniProt 27–392 Author chain MA； PDBConstruct 22–387； UniProt 27–392 Author chain N； PDBConstruct 22–387； UniProt 27–392 Author chain OA； PDBConstruct 22–387； UniProt 27–392 Author chain P； PDBConstruct 22–387； UniProt 27–392 Author chain QA； PDBConstruct 22–387； UniProt 27–392 Author chain R； PDBConstruct 22–387； UniProt 27–392 Author chain SA； PDBConstruct 22–387； UniProt 27–392 Author chain T； PDBConstruct 22–387； UniProt 27–392 Author chain UA； PDBConstruct 22–387； UniProt 27–392 Author chain W； PDBConstruct 22–387； UniProt 27–392 Author chain WA； PDBConstruct 22–387； UniProt 27–392 Author chain Y； PDBConstruct 22–387； UniProt 27–392

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	9ivp
Deposition date deposition_date	2024-07-24
Last revision last_revision	2025-06-04
Structure title title	24-mer DARPin-apoferritin scaffold in complex with the maltose binding protein
Keywords keywords	DARPin, apoferritin, scaffold, maltose binding protein, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

▼

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.

9ivp__assembly_1__model_1

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

Download this curve (.dat)

9ivp__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9ivp__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	99.17 Å
Rg (electron density)	99.25 Å
Total Rg	99.05 Å
Atom count	127848
Residues	16368
Excluded volume	2275000 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9ivp__assembly_1__model_1`	48-meric （48）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	DARPin,Ferritin heavy chain, N-terminally processed
Molecular weight formula_weight	41047.1 kDa
Source method src_method	man
Copy count entity_count	24

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E,G,I,K,M,O,Q,S,V,X,Z,BA,DA,FA,HA,JA,LA,NA,PA,RA,TA,VA
Atom count atom_count	128520

MGHHHHHHGPGSAKEEILEEIKKAKQEIAGGGGGSELGKELLEAARAGQDDEVRILMARGAEVNAADNTGTTPLHLAAYSGHLEIVEVLLKYGAEVNAADVFGYTPLHLAAYWGHLEIVEVLLKNGADVNARDSDGMTPLHLAAKWGHLEIVEVLLRYGADVEAQDKFGKTPFDLAIDNGNEDIAEVLQALLAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGAISLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDCNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGSGSGAEIEQAKKEIAYLIKK

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Maltodextrin-binding protein
Molecular weight formula_weight	45694.2 kDa
Source method src_method	man
Copy count entity_count	24

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F,H,J,L,N,P,R,T,W,Y,AA,CA,EA,GA,IA,KA,MA,OA,QA,SA,UA,WA

MGSSHHHHHHSSGLVPRGSHMKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNSSSNNNNNNNNNNLGIEGRENLYFQGGS

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

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

Resolution resolution	3.00 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	91926

24-mer DARPin-apoferritin scaffold in complex with the maltose binding protein

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

DARPin,Ferritin heavy chain, N-terminally processed

State in the Current Structure

Other States of the Same Protein in the Database

Maltodextrin-binding 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

9ivp__assembly_1__model_1

9ivp__assembly_1__model_1 | I(q)

9ivp__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

7. Citations (1)

24-mer DARPin-apoferritin scaffold in complex with the maltose binding protein

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

DARPin,Ferritin heavy chain, N-terminally processed

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Maltodextrin-binding 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

9ivp__assembly_1__model_1

9ivp__assembly_1__model_1 | I(q)

9ivp__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

7. Citations (1)