1wlp

Solution Structure Of The P22Phox-P47Phox Complex

Method: SOLUTION NMR Dmax: 62.4 Å Quality: GOOD

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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 148–167 Fragment:Alpha Polypeptide (1-25) Neutrophil cytosol factor 1 × 1 (P14598) SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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.

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 6–25; UniProt 148–167

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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 151–286 Fragment:Tandem SH3 domain Cytochrome b-245 light chain × 1 (P13498) SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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 B; PDBConstruct 3–138; UniProt 151–286

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 1wlp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1wlp
Deposition date deposition_date2004-06-29
Structure title titleSolution Structure Of The P22Phox-P47Phox Complex
Keywords keywordsSH3 domain, polyproline, OXIDOREDUCTASE-Signaling Protein COMPLEX; OXIDOREDUCTASE/Signaling Protein
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.94
Radius of gyration Rg (electron density) rg_electron16.89
Forward intensity I(0) i06090300.00
Molecular weight molecular_weight17922.0 kDa
Excluded volume excluded_volume22413 ų
Envelope volume envelope_volume27910 ų
Hydration-shell volume shell_volume14261 ų
Envelope diameter envelope_diameter62.0
Shell Rg shell_rg22.36
Envelope Rg envelope_rg17.47
Shape Rg shape_rg16.83
Total Rg total_rg18.03
Total atoms total_atoms2486
Residues n_residues163
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 dmax62.4
Rg (real space) rg_real17.92
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real6.0900e+06
I(0) uncertainty (real space) i0_real_error6.9040e+04
Rg (reciprocal space) rg_reciprocal17.92
I(0) (reciprocal space) i0_reciprocal6090000.0000
Solution quality estimate total_estimate0.8593
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.2
Skewness Skewness skewness0.345
Kurtosis Kurtosis kurtosis-0.168
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1436000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.732; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1wlpb1
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
Domain ID domain_idd1wlpb2
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
Domain ID domain_idd1wlpb3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id1wlpB01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains
Domain ID domain_id1wlpB02
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)