1k4u

Solution structure of the C-terminal SH3 domain of p67phox complexed with the C-terminal tail region of p47phox

Method: SOLUTION NMR Dmax: 43.1 Å Quality: GOOD

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

PHAGOCYTE NADPH OXIDASE SUBUNIT P67PHOX

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 S; UniProt 455–516 Fragment:C-TERMINAL SH3 DOMAIN (RESIDUES 455-516) Mutation:C499S/C514S PHAGOCYTE NADPH OXIDASE SUBUNIT P47PHOX × 1 (P14598) 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

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 8 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 S; PDBConstruct 1–62; UniProt 455–516

PHAGOCYTE NADPH OXIDASE SUBUNIT P47PHOX

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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain P; UniProt 359–390 Fragment:TAIL PEPTIDE (RESIDUES 359-390) PHAGOCYTE NADPH OXIDASE SUBUNIT P67PHOX × 1 (P19878) 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

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 2
Chains and sequence ranges Author chain P; PDBConstruct 1–32; UniProt 359–390

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 1k4u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1k4u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1k4u
Deposition date deposition_date2001-10-08
Structure title titleSolution structure of the C-terminal SH3 domain of p67phox complexed with the C-terminal tail region of p47phox
Keywords keywordsP67PHOX, P47PHOX, SH3-PEPTIDE COMPLEX, HELIX-TURN-HELIX, HORMONE-GROWTH FACTOR COMPLEX; HORMONE/GROWTH FACTOR
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.74
Radius of gyration Rg (electron density) rg_electron12.50
Forward intensity I(0) i0690810000.00
Molecular weight molecular_weight227630.0 kDa
Excluded volume excluded_volume287080 ų
Envelope volume envelope_volume24217 ų
Hydration-shell volume shell_volume13685 ų
Envelope diameter envelope_diameter51.4
Shell Rg shell_rg20.74
Envelope Rg envelope_rg15.47
Shape Rg shape_rg12.45
Total Rg total_rg12.84
Total atoms total_atoms32296
Residues n_residues2068
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 dmax43.1
Rg (real space) rg_real12.69
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real6.9080e+08
I(0) uncertainty (real space) i0_real_error7.3630e+06
Rg (reciprocal space) rg_reciprocal12.69
I(0) (reciprocal space) i0_reciprocal690800000.0000
Solution quality estimate total_estimate0.7811
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.7
Skewness Skewness skewness0.240
Kurtosis Kurtosis kurtosis-0.160
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha348900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.717; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1k4us_
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.2 — SH3-domain
Family Family familyb.34.2.1 — SH3-domain

CATH v4.4 (1 domains)

Domain ID domain_id1k4uS00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains

8. Citations (1)

9. Files and Curves (10)