SAXSdb — 6x91

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

Maltodextrin-binding protein, C->U-editing enzyme APOBEC-1 chimera

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 3	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 3 ZINC ION × 2 CACODYLATE ION × 2	Consistent with protein count
2	Insufficient information	Homooligomer	Protein 2 其他Polymer 4	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 4 ZINC ION × 2 CACODYLATE ION × 2	Consistent with protein count
3	Insufficient information	Homooligomer	Protein 2 其他Polymer 3	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 3 ZINC ION × 2 CACODYLATE ION × 2	Consistent with protein count
4	Insufficient information	Homooligomer	Protein 2 其他Polymer 4	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 4 ZINC ION × 2 CACODYLATE ION × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A4Z0THX4_ECOLX
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 Author chain E； PDBConstruct 2–367； UniProt 27–392 Author chain F； PDBConstruct 2–367； UniProt 27–392 Author chain G； PDBConstruct 2–367； UniProt 27–392 Author chain H； PDBConstruct 2–367； UniProt 27–392

Maltodextrin-binding protein, C->U-editing enzyme APOBEC-1 chimera

Homo sapiens

UniProt P41238

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 3	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 3 ZINC ION × 2 CACODYLATE ION × 2	Consistent with protein count
2	Insufficient information	Homooligomer	Protein 2 其他Polymer 4	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 4 ZINC ION × 2 CACODYLATE ION × 2	Consistent with protein count
3	Insufficient information	Homooligomer	Protein 2 其他Polymer 3	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 3 ZINC ION × 2 CACODYLATE ION × 2	Consistent with protein count
4	Insufficient information	Homooligomer	Protein 2 其他Polymer 4	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 4 ZINC ION × 2 CACODYLATE ION × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ABEC1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 372–593； UniProt 15–236 Author chain B； PDBConstruct 372–593； UniProt 15–236 Author chain C； PDBConstruct 372–593； UniProt 15–236 Author chain D； PDBConstruct 372–593； UniProt 15–236 Author chain E； PDBConstruct 372–593； UniProt 15–236 Author chain F； PDBConstruct 372–593； UniProt 15–236 Author chain G； PDBConstruct 372–593； UniProt 15–236 Author chain H； PDBConstruct 372–593； UniProt 15–236

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	6x91
Deposition date deposition_date	2020-06-02
Structure title title	Crystal structure of MBP-fused human APOBEC1
Keywords keywords	APOBEC, RNA editing, deamination, metalloenzyme, HYDROLASE; HYDROLASE
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.

6x91__assembly_1__model_1

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

Download this curve (.dat)

6x91__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6x91__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	43.27 Å
Rg (electron density)	43.75 Å
Total Rg	43.85 Å
Atom count	9531
Residues	1184
Excluded volume	170020 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6x91__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`6x91__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`6x91__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`6x91__assembly_4__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 (4)

Entity 1 Entity 1 polymer

Description description	Maltodextrin-binding protein, C->U-editing enzyme APOBEC-1 chimera
Molecular weight formula_weight	67073.3 kDa
EC 编号 ec_number	3.5.4.36
Mutation mutation	A338V,M46A,R48S,E63A,M80T,W121M,A146D,L173A,W199A,F205A
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	37624

MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELVKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNSSSRRRIEPWEFDVFYDPRELRKEACLLYEIKWGASSKIWRSSGKNTTNHVAVNFIKKFTSERDFHPSTSCSITWFLSWSPCWECSQAIREFLSRHPGVTLVIYVARLFAHMDQQNRQGLRDLVNSGVTIQIMRDSEYYHCWRNFVNYPPGDEAHWPQYPPAWMMLYALELHCIILSLPPCLKISRRAQNHLTAFRLHLQNCHYQTIPPHILLATGLIHPSVAWR

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 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	14

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 4 Entity 4 non-polymer

Description description	CACODYLATE ION
Molecular weight formula_weight	137.0 kDa
Source method src_method	syn
Copy count entity_count	8

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6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id	6x91A01
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	6x91B01
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	6x91C01
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	6x91E01
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	6x91F01
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	6x91G01
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

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Unit-cell length a length_a	177.715 Å
Unit-cell length b length_b	179.209 Å
Unit-cell length c length_c	210.505 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	32

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	3.510 Å
Low-resolution limit resolution_low	49.610 Å
R factor r_factor	0.2784
R_work r_work	0.2762
R_free r_free	0.2980

Crystal structure of MBP-fused human APOBEC1

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

Maltodextrin-binding protein, C->U-editing enzyme APOBEC-1 chimera

State in the Current Structure

Other States of the Same Protein in the Database

Maltodextrin-binding protein, C->U-editing enzyme APOBEC-1 chimera

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

6x91__assembly_1__model_1

6x91__assembly_1__model_1 | I(q)

6x91__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 (4)

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

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (1)

Crystal structure of MBP-fused human APOBEC1

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

Maltodextrin-binding protein, C->U-editing enzyme APOBEC-1 chimera

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, C->U-editing enzyme APOBEC-1 chimera

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

6x91__assembly_1__model_1

6x91__assembly_1__model_1 | I(q)

6x91__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 (4)

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

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (1)