SAXSdb — 2bpi

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

FE-SUPEROXIDE DISMUTASE

PLASMODIUM FALCIPARUM

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	FE (III) ION × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q8IAY6_PLAF7
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–198； UniProt 1–198 Author chain B； PDBConstruct 1–198； UniProt 1–198

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	2bpi
Deposition date deposition_date	2005-04-20
Structure title title	Structure of Iron dependent superoxide dismutase from P. falciparum.
Keywords keywords	DISMUTASE, OXIDOREDUCTASE, METAL-BINDING; OXIDOREDUCTASE
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.

2bpi__assembly_1__model_1

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

Download this curve (.dat)

2bpi__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2bpi__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	23.48 Å
Rg (electron density)	22.65 Å
Total Rg	23.72 Å
Atom count	3204
Residues	394
Excluded volume	56624 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2bpi__assembly_1__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 (3)

Entity 1 Entity 1 polymer

Description description	FE-SUPEROXIDE DISMUTASE
Molecular weight formula_weight	23831.7 kDa
EC 编号 ec_number	1.15.1.1
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3344

MVITLPKLKYALNALSPHISEETLNFHYNKHHAGYVNKLNTLIKDTPFAEKSLLDIVKESSGAIFNNAAQIWNHTFYWDSMGPDCGGEPHGEIKEKIQEDFGSFNNFKEQFSNILCGHFGSGWGWLALNNNNKLVILQTHDAGNPIKDNTGIPILTCDIWEHAYYIDYRNDRASYVKAWWNLVNWNFANENLKKAMQKLEHHHHHH

Source Source

Source organism organism	PLASMODIUM FALCIPARUM
NCBI taxonomy ID ncbi_taxonomy_id	36329
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	FE (III) ION
Molecular weight formula_weight	55.8 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	140

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2bpia1
Class class	a — All alpha proteins
Fold Fold fold	a.2 — Long alpha-hairpin
Superfamily Superfamily superfamily	a.2.11 — Fe,Mn superoxide dismutase (SOD), N-terminal domain
Family Family family	a.2.11.0 — automated matches

Domain ID domain_id	d2bpia2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.44 — Fe,Mn superoxide dismutase (SOD), C-terminal domain
Superfamily Superfamily superfamily	d.44.1 — Fe,Mn superoxide dismutase (SOD), C-terminal domain
Family Family family	d.44.1.0 — automated matches

Domain ID domain_id	d2bpib1
Class class	a — All alpha proteins
Fold Fold fold	a.2 — Long alpha-hairpin
Superfamily Superfamily superfamily	a.2.11 — Fe,Mn superoxide dismutase (SOD), N-terminal domain
Family Family family	a.2.11.0 — automated matches

Domain ID domain_id	d2bpib2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.44 — Fe,Mn superoxide dismutase (SOD), C-terminal domain
Superfamily Superfamily superfamily	d.44.1 — Fe,Mn superoxide dismutase (SOD), C-terminal domain
Family Family family	d.44.1.0 — automated matches

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Unit-cell length a length_a	55.941 Å
Unit-cell length b length_b	78.910 Å
Unit-cell length c length_c	90.621 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	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.520 Å
Low-resolution limit resolution_low	59.760 Å
R factor r_factor	0.1870
R_work r_work	0.1830
R_free r_free	0.2630

Structure of Iron dependent superoxide dismutase from P. falciparum.

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

FE-SUPEROXIDE DISMUTASE

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

2bpi__assembly_1__model_1

2bpi__assembly_1__model_1 | I(q)

2bpi__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

7. Citations (1)

Structure of Iron dependent superoxide dismutase from P. falciparum.

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

FE-SUPEROXIDE DISMUTASE

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

2bpi__assembly_1__model_1

2bpi__assembly_1__model_1 | I(q)

2bpi__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

7. Citations (1)