SAXSdb — 1ahn

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

FLAVODOXIN

Escherichia coli

UniProt P61949

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–175	Not recorded	CA CALCIUM ION × 1 FMN FLAVIN MONONUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7；PROTEIN WAS CRYSTALLIZED IN 30% MPD, 100 MM CACL2, 200 MM PIPES BUFFER, PH 7.0, 295 K.	Resolution 2.60 Å

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.

Other PDB	Difference from Current Entry 1AHN	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AG9 FLAVODOXINS THAT ARE REQUIRED FOR ENZYME ACTIVATION: THE STRUCTURE OF OXIDIZED FLAVODOXIN FROM ESCHERICHIA COLI AT 1.8 ANGSTROMS RESOLUTION. Deposited 1997-04-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–175（175 aa） Chain B 1–175（175 aa）	Not recorded	CA CALCIUM ION × 4 CL CHLORIDE ION × 2 NA SODIUM ION × 4 FMN FLAVIN MONONUCLEOTIDE × 2 BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；295 K；PROTEIN WAS CRYSTALLIZED BY MICROSEEDING IN 40% MPD, 100 MM CACL2, 20 MM BIS-TRIS, 10 MM IMIDAZOLE, PH 7.0, 295 K.	Resolution 1.80 Å R-free 0.250

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FLAV_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–175； UniProt 1–175

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	1ahn
Deposition date deposition_date	1997-04-07
Structure title title	E. COLI FLAVODOXIN AT 2.6 ANGSTROMS RESOLUTION
Keywords keywords	ELECTRON TRANSPORT, REDUCTIVE ACTIVATION, FLAVODOXIN, FLAVOPROTEIN; ELECTRON TRANSPORT
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	15.98 Å
Radius of gyration Rg (electron density) rg_electron	14.63 Å
Forward intensity I(0) i0	7155090.00
Molecular weight molecular_weight	19364.0 kDa
Excluded volume excluded_volume	24025 Å³
Envelope volume envelope_volume	25198 Å³
Hydration-shell volume shell_volume	14292 Å³
Envelope diameter envelope_diameter	48.7 Å
Shell Rg shell_rg	20.87 Å
Envelope Rg envelope_rg	14.90 Å
Shape Rg shape_rg	14.63 Å
Total Rg total_rg	15.73 Å
Total atoms total_atoms	1367
Residues n_residues	169
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	49.6 Å
Rg (real space) rg_real	15.85 Å
Rg uncertainty (real space) rg_real_error	0.24 Å
I(0) (real space) i0_real	7.1550e+06
I(0) uncertainty (real space) i0_real_error	7.4680e+04
Rg (reciprocal space) rg_reciprocal	15.87 Å
I(0) (reciprocal space) i0_reciprocal	7155000.0000
Solution quality estimate total_estimate	0.8970
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	21.3 Å
Skewness Skewness skewness	0.066
Kurtosis Kurtosis kurtosis	-0.442
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1068000.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.994

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	FLAVODOXIN
Molecular weight formula_weight	19623.7 kDa
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	1420

AITGIFFGSDTGNTENIAKMIQKQLGKDVADVHDIAKSSKEDLEAYDILLLGIPTWYYGEAQCDWDDFFPTLEEIDFNGKLVALFGCGDQEDYAEYFCDALGTIRDIIEPRGATIVGHWPTAGYHFEASKGLADDDHFVGLAIDEDRQPELTAERVEKWVKQISEELHLDEILNA

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

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 non-polymer

Description description	FLAVIN MONONUCLEOTIDE
Molecular weight formula_weight	456.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	53

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1ahna_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.23 — Flavodoxin-like
Superfamily Superfamily superfamily	c.23.5 — Flavoproteins
Family Family family	c.23.5.1 — Flavodoxin-related

CATH v4.4 (1 domains)

Domain ID domain_id	1ahnA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	360 — Flavodoxin domain

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8. Citations (1)

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Unit-cell length a length_a	78.830 Å
Unit-cell length b length_b	78.830 Å
Unit-cell length c length_c	52.070 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 3 1 2
Space-group number int_tables_number	149
Crystal system crystal_system	—

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.1900
R_work r_work	0.1900
R_free r_free	—

fit	/app/data/saxs_computation/ah/1ahn/1ahn.fit
pddf	/app/data/pr_computation/ah/1ahn/1ahn.pr.out
profile	/app/data/saxs_computation/ah/1ahn/1ahn.dat

E. COLI FLAVODOXIN AT 2.6 ANGSTROMS RESOLUTION

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

FLAVODOXIN

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction