1oey

Heterodimer of p40phox and p67phox PB1 domains from human NADPH oxidase

Method: X-RAY DIFFRACTION D_max: 129.6 Å Quality: GOOD

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

NEUTROPHIL CYTOSOL FACTOR 2

HOMO SAPIENS

UniProt P19878

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 352–429	Fragment：PB1 DOMAIN, RESIDUES 352-429 Non-standard monomer：Yes (specific site not provided by mmCIF)	NEUTROPHIL CYTOSOL FACTOR 4 × 1 （Q15080）	X-RAY DIFFRACTION X-ray crystallization conditions：pH 9；18% PEG 3350, 17% PEG 400, 4.8% ISOPROPYL ALCOHOL, 0.1 M CAPSO PH 9.0	Resolution 2.00 Å R-free 0.252
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 352–429	Fragment：PB1 DOMAIN, RESIDUES 352-429 Non-standard monomer：Yes (specific site not provided by mmCIF)	NEUTROPHIL CYTOSOL FACTOR 4 × 1 （Q15080）	X-RAY DIFFRACTION X-ray crystallization conditions：pH 9；18% PEG 3350, 17% PEG 400, 4.8% ISOPROPYL ALCOHOL, 0.1 M CAPSO PH 9.0	Resolution 2.00 Å R-free 0.252
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 352–429	Fragment：PB1 DOMAIN, RESIDUES 352-429 Non-standard monomer：Yes (specific site not provided by mmCIF)	NEUTROPHIL CYTOSOL FACTOR 4 × 1 （Q15080）	X-RAY DIFFRACTION X-ray crystallization conditions：pH 9；18% PEG 3350, 17% PEG 400, 4.8% ISOPROPYL ALCOHOL, 0.1 M CAPSO PH 9.0	Resolution 2.00 Å R-free 0.252
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 352–429	Fragment：PB1 DOMAIN, RESIDUES 352-429 Non-standard monomer：Yes (specific site not provided by mmCIF)	NEUTROPHIL CYTOSOL FACTOR 4 × 1 （Q15080）	X-RAY DIFFRACTION X-ray crystallization conditions：pH 9；18% PEG 3350, 17% PEG 400, 4.8% ISOPROPYL ALCOHOL, 0.1 M CAPSO PH 9.0	Resolution 2.00 Å R-free 0.252

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 1OEY	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1E96 Structure of the Rac/p67phox complex Deposited 2000-10-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–203（203 aa） Fragment：YES	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 10.5；0.1 M CAPS PH 10.5, 0.2 M LI ACETATE, 0.8 M NAH2PO4, 1.2 M K2HPO4	Resolution 2.40 Å R-free 0.284
1HH8 The active N-terminal region of p67phox: Structure at 1.8 Angstrom resolution and biochemical characterizations of the A128V mutant implicated in chronic granulomatous disease Deposited 2000-12-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–213（213 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1-213	Not recorded	FLC CITRATE ANION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.5；100 MM NA CITRATE PH 4.5, 17% PEG 2K MME, 10% GLYCEROL	Resolution 1.80 Å R-free 0.204
1K4U Solution structure of the C-terminal SH3 domain of p67phox complexed with the C-terminal tail region of p47phox Deposited 2001-10-08	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain S 455–516（62 aa） Fragment：C-TERMINAL SH3 DOMAIN (RESIDUES 455-516)	Mutation：C499S/C514S	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.1；298 K；Ionic strength (raw mmCIF value) 100mM KCl；Pressure 1 NMR sample composition 0.7mM p67SH3(C) U-15N,13C; 0.77mM p47 tail peptide; 5mM MOPSO buffer; 30 mM d10-DTT; 100mM KCl \| 90% H2O, 10% D2O; 100% D2O NMR sample composition 0.5mM p47 tail peptide U-15N,13C; 0.55mM p67SH3(C); 5mM MOPSO buffer; 30mM d10-DTT; 100mM KCl \| 90% H2O, 10% D2O; 100% D2O	Resolution not provided
1WM5 Crystal structure of the N-terminal TPR domain (1-203) of p67phox Deposited 2004-07-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–203（203 aa） Fragment：TPR domain	Not recorded	SO4 SULFATE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.9；277 K；ammonium sulfate, HEPES, pH 6.9, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 1.95 Å R-free 0.224
2DMO Refined solution structure of the 1st SH3 domain from human Neutrophil cytosol factor 2 (NCF-2) Deposited 2006-04-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 242–297（56 aa） Fragment：SH3 domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；296 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 1.3mM SH3 domain U-15N,13C; 20mM d-Tris HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O \| 90% H2O/10% D2O	Resolution not provided

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

View Construct and Data Evidence

UniProt name	NCF2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 6–83； UniProt 352–429 Author chain B； PDBConstruct 6–83； UniProt 352–429 Author chain C； PDBConstruct 6–83； UniProt 352–429 Author chain D； PDBConstruct 6–83； UniProt 352–429

NEUTROPHIL CYTOSOL FACTOR 4

HOMO SAPIENS

UniProt Q15080

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain J； UniProt 237–339	Fragment：PB1 DOMAIN, RESIDUES 237-339 Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	NEUTROPHIL CYTOSOL FACTOR 2 × 1 （P19878）	X-RAY DIFFRACTION X-ray crystallization conditions：pH 9；18% PEG 3350, 17% PEG 400, 4.8% ISOPROPYL ALCOHOL, 0.1 M CAPSO PH 9.0	Resolution 2.00 Å R-free 0.252
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain K； UniProt 237–339	Fragment：PB1 DOMAIN, RESIDUES 237-339 Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	NEUTROPHIL CYTOSOL FACTOR 2 × 1 （P19878）	X-RAY DIFFRACTION X-ray crystallization conditions：pH 9；18% PEG 3350, 17% PEG 400, 4.8% ISOPROPYL ALCOHOL, 0.1 M CAPSO PH 9.0	Resolution 2.00 Å R-free 0.252
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain L； UniProt 237–339	Fragment：PB1 DOMAIN, RESIDUES 237-339 Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	NEUTROPHIL CYTOSOL FACTOR 2 × 1 （P19878）	X-RAY DIFFRACTION X-ray crystallization conditions：pH 9；18% PEG 3350, 17% PEG 400, 4.8% ISOPROPYL ALCOHOL, 0.1 M CAPSO PH 9.0	Resolution 2.00 Å R-free 0.252
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain M； UniProt 237–339	Fragment：PB1 DOMAIN, RESIDUES 237-339 Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	NEUTROPHIL CYTOSOL FACTOR 2 × 1 （P19878）	X-RAY DIFFRACTION X-ray crystallization conditions：pH 9；18% PEG 3350, 17% PEG 400, 4.8% ISOPROPYL ALCOHOL, 0.1 M CAPSO PH 9.0	Resolution 2.00 Å R-free 0.252

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 1OEY	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1H6H Structure of the PX domain from p40phox bound to phosphatidylinositol 3-phosphate Deposited 2001-06-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–144（143 aa） Fragment：PX DOMAIN RESIDUES 2-144	Not recorded	PIB 2-(BUTANOYLOXY)-1-{[(HYDROXY{[2,3,4,6-TETRAHYDROXY-5-(PHOSPHONOOXY)CYCLOHEXYL]OXY}PHOSPHORYL)OXY]METHYL}ETHYL BUTANOATE × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；pH 7.50	Resolution 1.70 Å R-free 0.232
1W6X SH3 domain of p40phox, component of the NADPH oxidase Deposited 2004-08-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 174–228（55 aa） Fragment：SH3 DOMAIN, RESIDUES 174-228	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；287 K；VAPOR DIFFUSION AT 14 DEGRE C, PROTEIN AT 14 MG/ML, 20 MM HEPES PH 7.5, 150 MM NACL MIXED WITH 40% PEG2K MME, 100 MM AS 200 MM NA AC PH 4.6.	Resolution 2.00 Å R-free 0.250
1W6X SH3 domain of p40phox, component of the NADPH oxidase Deposited 2004-08-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 174–228（55 aa） Fragment：SH3 DOMAIN, RESIDUES 174-228	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；287 K；VAPOR DIFFUSION AT 14 DEGRE C, PROTEIN AT 14 MG/ML, 20 MM HEPES PH 7.5, 150 MM NACL MIXED WITH 40% PEG2K MME, 100 MM AS 200 MM NA AC PH 4.6.	Resolution 2.00 Å R-free 0.250
1W70 SH3 domain of p40phox complexed with C-terminal polyProline region of p47phox Deposited 2004-08-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 174–228（55 aa） Fragment：SH3 DOMAIN, RESIDUES 174-228	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；VAPOR DIFFUSION AT 20 DEGRE C AT 14MG/ML OF P40PHOX SH3 WITH A1/5 RATIO WITH POLYPROLINE PEPTIDE, 20 MM HEPES PH 7.5, 150 MM NACL MIXED WITH 100 MM NA-CITRATE/CITRIC ACID PH5, 2.4 M SA	Resolution 1.46 Å R-free 0.207
1W70 SH3 domain of p40phox complexed with C-terminal polyProline region of p47phox Deposited 2004-08-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 174–228（55 aa） Fragment：SH3 DOMAIN, RESIDUES 174-228	Not recorded	SO4 SULFATE ION × 3 TFA trifluoroacetic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；VAPOR DIFFUSION AT 20 DEGRE C AT 14MG/ML OF P40PHOX SH3 WITH A1/5 RATIO WITH POLYPROLINE PEPTIDE, 20 MM HEPES PH 7.5, 150 MM NACL MIXED WITH 100 MM NA-CITRATE/CITRIC ACID PH5, 2.4 M SA	Resolution 1.46 Å R-free 0.207
1Z9Q Solution structure of SH3 domain of p40phox Deposited 2005-04-04	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 168–233（66 aa） Fragment：SH3 domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 150mM NaCl；Pressure ambient NMR sample composition 0.5mM p40phoxSH3 U-13C, 15N; 50mM NaPi pH7.0; 150mM NaCl \| 90% H2O/10% D2O	Resolution not provided
2DYB The crystal structure of human p40(phox) Deposited 2006-09-08	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–339（339 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 6.5；293 K；5% PEG 20000, 200mM Bis-tris-HCl, 10mM sodium cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 3.15 Å R-free 0.302
2DYB The crystal structure of human p40(phox) Deposited 2006-09-08	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–339（339 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 6.5；293 K；5% PEG 20000, 200mM Bis-tris-HCl, 10mM sodium cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 3.15 Å R-free 0.302

5 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NCF4_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain J； PDBConstruct 5–107； UniProt 237–339 Author chain K； PDBConstruct 5–107； UniProt 237–339 Author chain L； PDBConstruct 5–107； UniProt 237–339 Author chain M； PDBConstruct 5–107； UniProt 237–339

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1oey
Deposition date deposition_date	2003-04-02
Structure title title	Heterodimer of p40phox and p67phox PB1 domains from human NADPH oxidase
Keywords keywords	IMMUNE SYSTEM, PB1 HETERODIMER-COMPLEX, NADPH OXIDASE, PB1 DOMAIN, HETERODIMERIZATION; IMMUNE SYSTEM
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	38.17 Å
Radius of gyration Rg (electron density) rg_electron	37.86 Å
Forward intensity I(0) i0	120626000.00
Molecular weight molecular_weight	86990.0 kDa
Excluded volume excluded_volume	108070 Å³
Envelope volume envelope_volume	156970 Å³
Hydration-shell volume shell_volume	36850 Å³
Envelope diameter envelope_diameter	138.0 Å
Shell Rg shell_rg	40.82 Å
Envelope Rg envelope_rg	37.36 Å
Shape Rg shape_rg	37.82 Å
Total Rg total_rg	38.18 Å
Total atoms total_atoms	6032
Residues n_residues	696
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	129.6 Å
Rg (real space) rg_real	38.28 Å
Rg uncertainty (real space) rg_real_error	1.44 Å
I(0) (real space) i0_real	1.2060e+08
I(0) uncertainty (real space) i0_real_error	2.1450e+06
Rg (reciprocal space) rg_reciprocal	38.21 Å
I(0) (reciprocal space) i0_reciprocal	120600000.0000
Solution quality estimate total_estimate	0.8579
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	50.6 Å
Skewness Skewness skewness	0.296
Kurtosis Kurtosis kurtosis	-0.397
Angular range angular_range	— – 0.2050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7925000.0000
Real-space data points n_real_points	42
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.923; Smooth: 0.671

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	NEUTROPHIL CYTOSOL FACTOR 2
Molecular weight formula_weight	9940.8 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	6382

GSHMAYTLKVHYKYTVVMKTQPGLPYSQVRDMVSKKLELRLEHTKLSYRPRDSNELVPLSEDSMKDAWGQVKNYCLTLWCENT

来源 Source

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	ESCHERICHIA COLI BL21(DE3)

Entity 2 Entity 2 polymer

Description description	NEUTROPHIL CYTOSOL FACTOR 4
Molecular weight formula_weight	12848.1 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J,K,L,M

GSHMTNWLRVYYYEDTISTIKDIAVEEDLSSTPLLKDLLELTRREFQREDIALNYRDAEGDLVRLLSDEDVALMVRQARGLPSQKRLFPWKLHITQKDNYRVYNTMP

来源 Source

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	ESCHERICHIA COLI BL21(DE3)

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	343

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7. Fold Classification (SCOP + CATH) 19 domains

SCOP 2.08 (11 domains)

Domain ID domain_id	d1oeya1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.2 — CAD & PB1 domains
Family Family family	d.15.2.2 — PB1 domain

Domain ID domain_id	d1oeya2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1oeyb1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.2 — CAD & PB1 domains
Family Family family	d.15.2.2 — PB1 domain

Domain ID domain_id	d1oeyb2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1oeyc_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.2 — CAD & PB1 domains
Family Family family	d.15.2.2 — PB1 domain

Domain ID domain_id	d1oeyd1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.2 — CAD & PB1 domains
Family Family family	d.15.2.2 — PB1 domain

Domain ID domain_id	d1oeyd2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1oeyj_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.2 — CAD & PB1 domains
Family Family family	d.15.2.2 — PB1 domain

Domain ID domain_id	d1oeyk_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.2 — CAD & PB1 domains
Family Family family	d.15.2.2 — PB1 domain

Domain ID domain_id	d1oeyl_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.2 — CAD & PB1 domains
Family Family family	d.15.2.2 — PB1 domain

Domain ID domain_id	d1oeym_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.2 — CAD & PB1 domains
Family Family family	d.15.2.2 — PB1 domain

CATH v4.4 (8 domains)

Domain ID domain_id	1oeyA00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Domain ID domain_id	1oeyB00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Domain ID domain_id	1oeyC00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Domain ID domain_id	1oeyD00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Domain ID domain_id	1oeyJ00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Domain ID domain_id	1oeyK00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Domain ID domain_id	1oeyL00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Domain ID domain_id	1oeyM00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

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8. Citations (1)

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Unit-cell length a length_a	151.422 Å
Unit-cell length b length_b	151.422 Å
Unit-cell length c length_c	68.317 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	24

Space group space_group	P 64
Space-group number int_tables_number	172
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	100.000 Å
R factor r_factor	0.2120
R_work r_work	0.2100
R_free r_free	0.2520

fit	/app/data/saxs_computation/oe/1oey/1oey.fit
pddf	/app/data/pr_computation/oe/1oey/1oey.pr.out
profile	/app/data/saxs_computation/oe/1oey/1oey.dat

Heterodimer of p40phox and p67phox PB1 domains from human NADPH oxidase

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

NEUTROPHIL CYTOSOL FACTOR 2

State in the Current Structure

Other States of the Same Protein in the Database

NEUTROPHIL CYTOSOL FACTOR 4

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 19 domains

SCOP 2.08 (11 domains)

CATH v4.4 (8 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)