5a63

Cryo-EM structure of the human gamma-secretase complex at 3.4 angstrom resolution.

Method: ELECTRON MICROSCOPY Dmax: 132.7 Å Quality: GOOD

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

Nicastrin

Homo sapiens

UniProt Q92542

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 6 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–709 Not recorded Presenilin-1 × 1 (P49768) Gamma-secretase subunit APH-1A × 1 (Q96BI3) Gamma-secretase subunit PEN-2 × 1 (Q9NZ42) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:25 MM HEPES, PH 7.4, 150 MM NACL AND AMPHIPOL A8-35;pH 7.4;25 MM HEPES, PH 7.4, 150 MM NACL AND AMPHIPOL A8-35 cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 100, TEMPERATURE- 85, INSTRUMENT- FEI VITROBOT MARK IV, METHOD- BLOT FOR 4 SECONDS BEFORE PLUNGING, Resolution 3.40 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NICA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–709; UniProt 1–709

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 Other combination Heteromer Protein × 4 其他Polymer 6 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–467 Not recorded Nicastrin × 1 (Q92542) Gamma-secretase subunit APH-1A × 1 (Q96BI3) Gamma-secretase subunit PEN-2 × 1 (Q9NZ42) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:25 MM HEPES, PH 7.4, 150 MM NACL AND AMPHIPOL A8-35;pH 7.4;25 MM HEPES, PH 7.4, 150 MM NACL AND AMPHIPOL A8-35 cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 100, TEMPERATURE- 85, INSTRUMENT- FEI VITROBOT MARK IV, METHOD- BLOT FOR 4 SECONDS BEFORE PLUNGING, Resolution 3.40 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.

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–467; UniProt 1–467

Gamma-secretase subunit APH-1A

Homo sapiens

UniProt Q96BI3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 6 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–265 Not recorded Nicastrin × 1 (Q92542) Presenilin-1 × 1 (P49768) Gamma-secretase subunit PEN-2 × 1 (Q9NZ42) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:25 MM HEPES, PH 7.4, 150 MM NACL AND AMPHIPOL A8-35;pH 7.4;25 MM HEPES, PH 7.4, 150 MM NACL AND AMPHIPOL A8-35 cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 100, TEMPERATURE- 85, INSTRUMENT- FEI VITROBOT MARK IV, METHOD- BLOT FOR 4 SECONDS BEFORE PLUNGING, Resolution 3.40 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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name APH1A_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–265; UniProt 1–265

Gamma-secretase subunit PEN-2

Homo sapiens

UniProt Q9NZ42

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 6 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–101 Not recorded Nicastrin × 1 (Q92542) Presenilin-1 × 1 (P49768) Gamma-secretase subunit APH-1A × 1 (Q96BI3) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:25 MM HEPES, PH 7.4, 150 MM NACL AND AMPHIPOL A8-35;pH 7.4;25 MM HEPES, PH 7.4, 150 MM NACL AND AMPHIPOL A8-35 cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 100, TEMPERATURE- 85, INSTRUMENT- FEI VITROBOT MARK IV, METHOD- BLOT FOR 4 SECONDS BEFORE PLUNGING, Resolution 3.40 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.

26 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PEN2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–101; UniProt 1–101

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 5a63

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5a63
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5a63
Deposition date deposition_date2015-06-24
Structure title titleCryo-EM structure of the human gamma-secretase complex at 3.4 angstrom resolution.
Keywords keywordsHYDROLASE, CRYO-EM, HUMAN GAMMA-SECRETASE, MEMBRANE PROTEIN; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.71
Radius of gyration Rg (electron density) rg_electron38.41
Forward intensity I(0) i0262769000.00
Molecular weight molecular_weight141560.0 kDa
Excluded volume excluded_volume181050 ų
Envelope volume envelope_volume233680 ų
Hydration-shell volume shell_volume50750 ų
Envelope diameter envelope_diameter136.6
Shell Rg shell_rg44.09
Envelope Rg envelope_rg38.07
Shape Rg shape_rg38.39
Total Rg total_rg38.85
Total atoms total_atoms10003
Residues n_residues1223
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 dmax132.7
Rg (real space) rg_real38.85
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real2.6280e+08
I(0) uncertainty (real space) i0_real_error4.4840e+06
Rg (reciprocal space) rg_reciprocal38.77
I(0) (reciprocal space) i0_reciprocal262700000.0000
Solution quality estimate total_estimate0.8780
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.1
Skewness Skewness skewness0.390
Kurtosis Kurtosis kurtosis-0.431
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha31310000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; Smooth: 0.901

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)