3ulr

Lysozyme contamination facilitates crystallization of a hetero-trimericCortactin:Arg:Lysozyme complex

Method: X-RAY DIFFRACTION Dmax: 62.0 Å Quality: REASONABLE

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

Lysozyme C

Gallus gallus

UniProt P00698

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 19–147 Not recorded Src substrate cortactin × 1 (Q60598) Abelson tyrosine-protein kinase 2 × 1 (P42684) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;297 K;1.0M Na Citrate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 297K Resolution 1.65 Å R-free 0.225

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.

1320 other PDB entries and 1450 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LYSC_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–129; UniProt 19–147

Src substrate cortactin

Mus musculus

UniProt Q60598

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 487–546 Fragment:SH3 domain (UNP residues 487-546) Lysozyme C × 1 (P00698) Abelson tyrosine-protein kinase 2 × 1 (P42684) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;297 K;1.0M Na Citrate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 297K Resolution 1.65 Å R-free 0.225

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 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SRC8_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–65; UniProt 487–546

Abelson tyrosine-protein kinase 2

OrganismNot specified

UniProt P42684

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 563–579 Fragment:PXXP1 (UNP residues 563-579) Lysozyme C × 1 (P00698) Src substrate cortactin × 1 (Q60598) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;297 K;1.0M Na Citrate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 297K Resolution 1.65 Å R-free 0.225

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.

8 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ABL2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–17; UniProt 563–579

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 3ulr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ulr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ulr
Deposition date deposition_date2011-11-11
Structure title titleLysozyme contamination facilitates crystallization of a hetero-trimericCortactin:Arg:Lysozyme complex
Keywords keywordsSH3, Protein-protein interaction, HYDROLASE, PROTEIN BINDING; HYDROLASE, PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.62
Radius of gyration Rg (electron density) rg_electron17.65
Forward intensity I(0) i010246800.00
Molecular weight molecular_weight22818.0 kDa
Excluded volume excluded_volume28155 ų
Envelope volume envelope_volume33103 ų
Hydration-shell volume shell_volume16069 ų
Envelope diameter envelope_diameter61.3
Shell Rg shell_rg23.25
Envelope Rg envelope_rg17.94
Shape Rg shape_rg17.64
Total Rg total_rg18.53
Total atoms total_atoms1602
Residues n_residues206
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 dmax62.0
Rg (real space) rg_real18.60
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real1.0250e+07
I(0) uncertainty (real space) i0_real_error1.3080e+05
Rg (reciprocal space) rg_reciprocal18.60
I(0) (reciprocal space) i0_reciprocal10250000.0000
Solution quality estimate total_estimate0.6787
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.4
Skewness Skewness skewness0.347
Kurtosis Kurtosis kurtosis-0.336
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha2633000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.989; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3ulrb1
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.2 — SH3-domain
Family Family familyb.34.2.0 — automated matches
Domain ID domain_idd3ulrb2
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_id3ulrA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10
Domain ID domain_id3ulrB00
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)