9boi

Cryo-EM structure of human Spns1 in complex with LPC (18:1)

Method: ELECTRON MICROSCOPY Dmax: 74.2 Å Quality: GOOD

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

mVenus,Maltose/maltodextrin-binding periplasmic protein,Protein spinster homolog 1,Designed ankyrin repeat protein (DARPin)

Homo sapiens

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 29–391 Not recorded 42H (4R,7R,18Z)-4,7-dihydroxy-N,N,N-trimethyl-10-oxo-3,5,9-trioxa-4-phosphaheptacos-18-en-1-aminium 4-oxide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 5.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.22 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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 248–610; UniProt 29–391

mVenus,Maltose/maltodextrin-binding periplasmic protein,Protein spinster homolog 1,Designed ankyrin repeat protein (DARPin)

Homo sapiens

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–238 Not recorded 42H (4R,7R,18Z)-4,7-dihydroxy-N,N,N-trimethyl-10-oxo-3,5,9-trioxa-4-phosphaheptacos-18-en-1-aminium 4-oxide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 5.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.22 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–239; UniProt 2–238

mVenus,Maltose/maltodextrin-binding periplasmic protein,Protein spinster homolog 1,Designed ankyrin repeat protein (DARPin)

Homo sapiens

UniProt Q9H2V7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 56–528 Not recorded 42H (4R,7R,18Z)-4,7-dihydroxy-N,N,N-trimethyl-10-oxo-3,5,9-trioxa-4-phosphaheptacos-18-en-1-aminium 4-oxide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 5.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.22 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.

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

View Construct and Data Evidence
UniProt name SPNS1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 625–1097; UniProt 56–528

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 9boi

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9boi
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9boi
Deposition date deposition_date2024-05-03
Structure title titleCryo-EM structure of human Spns1 in complex with LPC (18:1)
Keywords keywordslysosome, major facilitator superfamily, lysophospholipid transporter, lysophosphatidylcholine, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier22.90
Radius of gyration Rg (electron density) rg_electron21.93
Forward intensity I(0) i030846900.00
Molecular weight molecular_weight46104.0 kDa
Excluded volume excluded_volume59240 ų
Envelope volume envelope_volume69865 ų
Hydration-shell volume shell_volume26232 ų
Envelope diameter envelope_diameter76.0
Shell Rg shell_rg29.28
Envelope Rg envelope_rg22.15
Shape Rg shape_rg21.93
Total Rg total_rg22.88
Total atoms total_atoms3256
Residues n_residues423
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 dmax74.2
Rg (real space) rg_real22.84
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real3.0850e+07
I(0) uncertainty (real space) i0_real_error4.5700e+05
Rg (reciprocal space) rg_reciprocal22.86
I(0) (reciprocal space) i0_reciprocal30850000.0000
Solution quality estimate total_estimate0.8157
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.4
Skewness Skewness skewness0.286
Kurtosis Kurtosis kurtosis-0.330
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5301000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)