10tp

ArsB from L. ferriphilum in inward-facing state (parallel dimer)

Method: ELECTRON MICROSCOPY Dmax: 110.1 Å Quality: GOOD

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

Arsenical pump membrane protein

Leptospirillum ferriphilum

UniProt J9ZEP4

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–428 Chain B; UniProt 1–428 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name J9ZEP4_LEPFM
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–428; UniProt 1–428 Author chain B; PDBConstruct 1–428; UniProt 1–428

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

SAXS profile for 10tp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10tp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10tp
Deposition date deposition_date2026-02-08
Structure title titleArsB from L. ferriphilum in inward-facing state (parallel dimer)
Keywords keywordsarsenite, membrane transporter, secondary transporter, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.12
Radius of gyration Rg (electron density) rg_electron33.59
Forward intensity I(0) i099301100.00
Molecular weight molecular_weight90491.0 kDa
Excluded volume excluded_volume118050 ų
Envelope volume envelope_volume147100 ų
Hydration-shell volume shell_volume37238 ų
Envelope diameter envelope_diameter111.2
Shell Rg shell_rg39.65
Envelope Rg envelope_rg32.80
Shape Rg shape_rg33.60
Total Rg total_rg34.07
Total atoms total_atoms6402
Residues n_residues856
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax110.1
Rg (real space) rg_real34.16
Rg uncertainty (real space) rg_real_error0.96
I(0) (real space) i0_real9.9300e+07
I(0) uncertainty (real space) i0_real_error1.8280e+06
Rg (reciprocal space) rg_reciprocal34.14
I(0) (reciprocal space) i0_reciprocal99300000.0000
Solution quality estimate total_estimate0.8925
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.5
Skewness Skewness skewness0.262
Kurtosis Kurtosis kurtosis-0.719
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15430000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.902

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)