1bg7

LOCALIZED UNFOLDING AT THE JUNCTION OF THREE FERRITIN SUBUNITS. A MECHANISM FOR IRON RELEASE?

Method: X-RAY DIFFRACTION D_max: 71.2 Å Quality: GOOD

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

FERRITIN

Rana catesbeiana

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain A； UniProt 1–176	Mutation：K82Q, L134P	CA CALCIUM ION × 24	X-RAY DIFFRACTION X-ray crystallization conditions：pH 4.6；pH 4.6	Resolution 1.85 Å R-free 0.233

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	FRI1_RANCA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–176； UniProt 1–176

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1bg7
Deposition date deposition_date	1998-06-05
Structure title title	LOCALIZED UNFOLDING AT THE JUNCTION OF THREE FERRITIN SUBUNITS. A MECHANISM FOR IRON RELEASE?
Keywords keywords	FERRITIN, IRON STORAGE; IRON STORAGE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	18.92 Å
Radius of gyration Rg (electron density) rg_electron	17.99 Å
Forward intensity I(0) i0	6297380.00
Molecular weight molecular_weight	17608.0 kDa
Excluded volume excluded_volume	21769 Å³
Envelope volume envelope_volume	26408 Å³
Hydration-shell volume shell_volume	13452 Å³
Envelope diameter envelope_diameter	69.0 Å
Shell Rg shell_rg	22.82 Å
Envelope Rg envelope_rg	18.55 Å
Shape Rg shape_rg	17.97 Å
Total Rg total_rg	18.88 Å
Total atoms total_atoms	1235
Residues n_residues	153
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	71.2 Å
Rg (real space) rg_real	19.11 Å
Rg uncertainty (real space) rg_real_error	0.64 Å
I(0) (real space) i0_real	6.2970e+06
I(0) uncertainty (real space) i0_real_error	8.6450e+04
Rg (reciprocal space) rg_reciprocal	19.08 Å
I(0) (reciprocal space) i0_reciprocal	6297000.0000
Solution quality estimate total_estimate	0.7773
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	18.8 Å
Skewness Skewness skewness	0.623
Kurtosis Kurtosis kurtosis	0.001
Angular range angular_range	— – 0.4200 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1191000.0000
Real-space data points n_real_points	73
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.511; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.569; Smooth: 0.999

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	FERRITIN
Molecular weight formula_weight	20546.1 kDa
Mutation mutation	K82Q, L134P
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1267

MDSQVRQNFHRDCEAAINRMVNMELYASYTYLSMAFYFDRDDIALHNVAKFFKEQSHEEREHAEKLMKDQNKRGGRIVLQDVQKPERDEWGNTLEAMQAALQLEKTVNQALLDLHKVGSDKVDPHLCDFLETEYPEEQVKSIKQLGDYITNLKRLGLPQNGMGEYLFDKHTMGESS

来源 Source

来源生物 organism	Rana catesbeiana
通用名 common_name	bullfrog
NCBI Class编号 ncbi_taxonomy_id	8400
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	32

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1bg7a_
Class class	a — All alpha proteins
Fold Fold fold	a.25 — Ferritin-like
Superfamily Superfamily superfamily	a.25.1 — Ferritin-like
Family Family family	a.25.1.1 — Ferritin

CATH v4.4 (1 domains)

Domain ID domain_id	1bg7A00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1260 — Ferritin
Homologous superfamily homologous superfamily	10 — Ferritin, core subunit, four-helix bundle

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8. Citations (1)

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Unit-cell length a length_a	182.800 Å
Unit-cell length b length_b	182.800 Å
Unit-cell length c length_c	182.800 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	96

Space group space_group	F 4 3 2
Space-group number int_tables_number	209
Crystal system crystal_system	—

Resolution resolution	1.850 Å
Low-resolution limit resolution_low	40.000 Å
R factor r_factor	0.2070
R_work r_work	0.2070
R_free r_free	0.2330

fit	/app/data/saxs_computation/bg/1bg7/1bg7.fit
pddf	/app/data/pr_computation/bg/1bg7/1bg7.pr.out
profile	/app/data/saxs_computation/bg/1bg7/1bg7.dat