2kr6

Solution structure of presenilin-1 CTF subunit

Method: SOLUTION NMR Dmax: 211.6 Å Quality: REASONABLE

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

Presenilin-1

Homo sapiens

UniProt P49768

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 292–467 Fragment:Presenilin-1 CTF subunit, UNP residues 292-467 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.8;313 K;Ionic strength (raw mmCIF value) 20;Pressure AMBIENT NMR sample composition:0.5 mM [U-99% 13C; U-99% 15N] ps1ctf-1, 90% H2O/10% D2O | 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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSN1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–176; UniProt 292–467

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 2kr6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2kr6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2kr6
Deposition date deposition_date2009-12-04
Structure title titleSolution structure of presenilin-1 CTF subunit
Keywords keywords;protease, Alternative splicing, Alzheimer disease, Amyloidosis, Apoptosis, Cell adhesion, Disease mutation, Endoplasmic reticulum, Golgi apparatus, Hydrolase, Membrane, Neurodegeneration, Notch signaling pathway, Phosphoprotein, Polymorphism, Transmembrane ;; HYDROLASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier41.31
Radius of gyration Rg (electron density) rg_electron41.14
Forward intensity I(0) i02046710000.00
Molecular weight molecular_weight388040.0 kDa
Excluded volume excluded_volume487260 ų
Envelope volume envelope_volume456890 ų
Hydration-shell volume shell_volume67953 ų
Envelope diameter envelope_diameter223.2
Shell Rg shell_rg51.10
Envelope Rg envelope_rg66.30
Shape Rg shape_rg40.97
Total Rg total_rg41.97
Total atoms total_atoms54020
Residues n_residues3520
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 dmax211.6
Rg (real space) rg_real43.03
Rg uncertainty (real space) rg_real_error6.44
I(0) (real space) i0_real2.0470e+09
I(0) uncertainty (real space) i0_real_error4.9780e+07
Rg (reciprocal space) rg_reciprocal41.32
I(0) (reciprocal space) i0_reciprocal2043000000.0000
Solution quality estimate total_estimate0.6154
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks6
Primary peak position r_peak_primary22.3
Skewness Skewness skewness0.925
Kurtosis Kurtosis kurtosis0.013
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1482000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.000; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.000; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2kr6A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology472 — Cyclin A; domain 1
Homologous superfamily homologous superfamily100 — Presenilin

8. Citations (1)

9. Files and Curves (10)