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1szv

Structure of the Adaptor Protein p14 reveals a Profilin-like Fold with Novel Function

Method: SOLUTION NMR Dmax: 47.0 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Late endosomal/lysosomal Mp1 interacting protein

Mus musculus

UniProt Q9JHS3

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 1–125 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.5；298 K；Ionic strength (raw mmCIF value) 250mM NaCl；Pressure ambient NMR sample composition：0.3mM P14 U-15N,13C; 50mM phosphate | 90% H2O/10% D2O NMR sample composition：0.3mM P14 U-15N,13C; 50mM phosphate | 100% D2O NMR sample composition：0.3mM P14 U-2H,15N,13C; 50mM phosphate | 90% H2O/10% D2O Resolution not provided

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 1SZV Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1SKO MP1-p14 Complex Deposited 2004-03-05 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 2–124（123 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；293 K；14% PEG 3350, 0.1M Tris-HCl buffer, pH 9.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.00 Å R-free 0.271
1VET Crystal Structure of p14/MP1 at 1.9 A resolution Deposited 2004-04-05 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–125（125 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；292 K；PEG4000, Tris, Magnesium Chloride, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 1.90 Å R-free 0.259
1VEU Crystal structure of the p14/MP1 complex at 2.15 A resolution Deposited 2004-04-05 Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–125（125 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；292 K；PEG4000, Tris, Magnesium Chloride, Sodium/Potassium Phosphate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.15 Å R-free 0.262
2ZL1 MP1-p14 Scaffolding complex Deposited 2008-04-02 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 2–125（124 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；295 K；11%(w/v) PEG 3350, 0.1M HEPES, pH 7.5, vapor diffusion, hanging drop, temperature 295K
Resolution 2.00 Å R-free 0.256
3CPT MP1-p14 Scaffolding complex Deposited 2008-04-01 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 2–125（124 aa）
Mutation：Y56A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；295 K；10%(w/v) PEG 3350, 0.1 M HEPES, pH 7.5, vapor diffusion, hanging drop, temperature 295K
Resolution 1.90 Å R-free 0.277

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LM1P_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 6–130； UniProt 1–125

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 1szv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1szv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1szv
Deposition date deposition_date2004-04-06
Structure title titleStructure of the Adaptor Protein p14 reveals a Profilin-like Fold with Novel Function
Keywords keywordsP14, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.16 Å
Radius of gyration Rg (electron density) rg_electron13.65 Å
Forward intensity I(0) i03712790.00
Molecular weight molecular_weight13480.0 kDa
Excluded volume excluded_volume16874 ų
Envelope volume envelope_volume19210 ų
Hydration-shell volume shell_volume11944 ų
Envelope diameter envelope_diameter45.8 Å
Shell Rg shell_rg19.46 Å
Envelope Rg envelope_rg13.96 Å
Shape Rg shape_rg13.65 Å
Total Rg total_rg14.88 Å
Total atoms total_atoms1895
Residues n_residues125
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax47.0 Å
Rg (real space) rg_real15.05 Å
Rg uncertainty (real space) rg_real_error0.25 Å
I(0) (real space) i0_real3.7130e+06
I(0) uncertainty (real space) i0_real_error3.9220e+04
Rg (reciprocal space) rg_reciprocal15.06 Å
I(0) (reciprocal space) i0_reciprocal3713000.0000
Solution quality estimate total_estimate0.9005
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.6 Å
Skewness Skewness skewness0.092
Kurtosis Kurtosis kurtosis-0.446
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha706500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.985
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1szva_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.110 — Profilin-like
Superfamily Superfamily superfamilyd.110.7 — Roadblock/LC7 domain
Family Family familyd.110.7.1 — Roadblock/LC7 domain

CATH v4.4 (1 domains)

Domain ID domain_id1szvA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily30 — Dynein light chain 2a, cytoplasmic
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8. Citations (1)

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9. Files and Curves (10)