8wej

Structure of human phagocyte NADPH oxidase in the activated state

Method: ELECTRON MICROSCOPY Dmax: 185.1 Å Quality: REASONABLE

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

Cytochrome b-245 light chain

Homo sapiens

UniProt P13498

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 × 7 其他Polymer 1 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–195 Not recorded Cytochrome b-245 heavy chain × 1 (P04839) Neutrophil cytosol factor 1 × 1 (P14598) Neutrophil cytosolic factor 2 (65kDa, chronic granulomatous disease, autosomal 2), isoform CRA_a × 1 (A0A024R936) Rac family small GTPase 1 × 1 (A0A8C8XFZ1) 7D5 Fab heavy chain × 1 7D5 Fab light chain × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MG MAGNESIUM ION × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 FDA DIHYDROFLAVINE-ADENINE DINUCLEOTIDE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CY24A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–195; UniProt 1–195

Cytochrome b-245 heavy chain

Homo sapiens

UniProt P04839

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 × 7 其他Polymer 1 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 1–570 Not recorded Cytochrome b-245 light chain × 1 (P13498) Neutrophil cytosol factor 1 × 1 (P14598) Neutrophil cytosolic factor 2 (65kDa, chronic granulomatous disease, autosomal 2), isoform CRA_a × 1 (A0A024R936) Rac family small GTPase 1 × 1 (A0A8C8XFZ1) 7D5 Fab heavy chain × 1 7D5 Fab light chain × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MG MAGNESIUM ION × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 FDA DIHYDROFLAVINE-ADENINE DINUCLEOTIDE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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.

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

View Construct and Data Evidence
UniProt name CY24B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–570; UniProt 1–570

Neutrophil cytosol factor 1

Homo sapiens

UniProt P14598

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 × 7 其他Polymer 1 PDB declaration: heptameric(7) Consistent with protein copy count Chain C; UniProt 1–286 Not recorded Cytochrome b-245 light chain × 1 (P13498) Cytochrome b-245 heavy chain × 1 (P04839) Neutrophil cytosolic factor 2 (65kDa, chronic granulomatous disease, autosomal 2), isoform CRA_a × 1 (A0A024R936) Rac family small GTPase 1 × 1 (A0A8C8XFZ1) 7D5 Fab heavy chain × 1 7D5 Fab light chain × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MG MAGNESIUM ION × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 FDA DIHYDROFLAVINE-ADENINE DINUCLEOTIDE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NCF1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–286; UniProt 1–286

Neutrophil cytosolic factor 2 (65kDa, chronic granulomatous disease, autosomal 2), isoform CRA_a

Homo sapiens

UniProt A0A024R936

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 × 7 其他Polymer 1 PDB declaration: heptameric(7) Consistent with protein copy count Chain D; UniProt 1–306 Not recorded Cytochrome b-245 light chain × 1 (P13498) Cytochrome b-245 heavy chain × 1 (P04839) Neutrophil cytosol factor 1 × 1 (P14598) Rac family small GTPase 1 × 1 (A0A8C8XFZ1) 7D5 Fab heavy chain × 1 7D5 Fab light chain × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MG MAGNESIUM ION × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 FDA DIHYDROFLAVINE-ADENINE DINUCLEOTIDE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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 A0A024R936_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–306; UniProt 1–306

Rac family small GTPase 1

Homo sapiens

UniProt A0A8C8XFZ1

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 × 7 其他Polymer 1 PDB declaration: heptameric(7) Consistent with protein copy count Chain E; UniProt 1–192 Not recorded Cytochrome b-245 light chain × 1 (P13498) Cytochrome b-245 heavy chain × 1 (P04839) Neutrophil cytosol factor 1 × 1 (P14598) Neutrophil cytosolic factor 2 (65kDa, chronic granulomatous disease, autosomal 2), isoform CRA_a × 1 (A0A024R936) 7D5 Fab heavy chain × 1 7D5 Fab light chain × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MG MAGNESIUM ION × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 FDA DIHYDROFLAVINE-ADENINE DINUCLEOTIDE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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 A0A8C8XFZ1_PANLE
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–192; UniProt 1–192

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 8wej

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8wej
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8wej
Deposition date deposition_date2023-09-18
Structure title titleStructure of human phagocyte NADPH oxidase in the activated state
Keywords keywordsNOX2, p22, CYBA, CYBB, TP1170, NOX, p67, Rac, p47, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.95
Radius of gyration Rg (electron density) rg_electron50.08
Forward intensity I(0) i0313699000.00
Molecular weight molecular_weight151170.0 kDa
Excluded volume excluded_volume191210 ų
Envelope volume envelope_volume248330 ų
Hydration-shell volume shell_volume47549 ų
Envelope diameter envelope_diameter191.1
Shell Rg shell_rg44.73
Envelope Rg envelope_rg50.17
Shape Rg shape_rg50.07
Total Rg total_rg49.87
Total atoms total_atoms10658
Residues n_residues1336
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 dmax185.1
Rg (real space) rg_real50.14
Rg uncertainty (real space) rg_real_error3.09
I(0) (real space) i0_real3.1370e+08
I(0) uncertainty (real space) i0_real_error7.0270e+06
Rg (reciprocal space) rg_reciprocal48.96
I(0) (reciprocal space) i0_reciprocal313200000.0000
Solution quality estimate total_estimate0.7067
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.7
Skewness Skewness skewness0.681
Kurtosis Kurtosis kurtosis-0.151
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15090000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.452; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.280; Smooth: 0.547

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

8. Citations (1)

9. Files and Curves (10)