3bu3

Crystal structure of the insulin receptor kinase in complex with IRS2 KRLB peptide

Method: X-RAY DIFFRACTION Dmax: 61.7 Å Quality: EXCELLENT

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

insulin receptor subunit beta

Homo sapiens

UniProt P06213

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 1005–1310 Fragment:protein kinase Non-standard monomer:Yes (specific site not provided by mmCIF) Insulin receptor substrate 2 × 1 (P81122) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;28% PEG8000 0.1 M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.65 Å R-free 0.220

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.

85 other PDB entries and 99 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INSR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–306; UniProt 1005–1310

Insulin receptor substrate 2

OrganismNot specified

UniProt P81122

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 620–634 Fragment:UNP residues 620-634 insulin receptor subunit beta × 1 (P06213) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;28% PEG8000 0.1 M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.65 Å R-free 0.220

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IRS2_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–15; UniProt 620–634

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 3bu3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3bu3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3bu3
Deposition date deposition_date2007-12-31
Structure title titleCrystal structure of the insulin receptor kinase in complex with IRS2 KRLB peptide
Keywords keywords;IRK, KRLB, IRS2, insulin receptor, substrate, Alternative splicing, ATP-binding, Carbohydrate metabolism, Cleavage on pair of basic residues, Diabetes mellitus, Disease mutation, Glycoprotein, Kinase, Membrane, Nucleotide-binding, Phosphoprotein, Polymorphism, Transferase, Transmembrane, Tyrosine-protein kinase, Transducer ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.22
Radius of gyration Rg (electron density) rg_electron19.03
Forward intensity I(0) i022087800.00
Molecular weight molecular_weight34978.0 kDa
Excluded volume excluded_volume43429 ų
Envelope volume envelope_volume50894 ų
Hydration-shell volume shell_volume21805 ų
Envelope diameter envelope_diameter62.6
Shell Rg shell_rg25.83
Envelope Rg envelope_rg19.31
Shape Rg shape_rg19.03
Total Rg total_rg19.96
Total atoms total_atoms2452
Residues n_residues308
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 dmax61.7
Rg (real space) rg_real20.09
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real2.2090e+07
I(0) uncertainty (real space) i0_real_error2.8150e+05
Rg (reciprocal space) rg_reciprocal20.11
I(0) (reciprocal space) i0_reciprocal22090000.0000
Solution quality estimate total_estimate0.9028
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.143
Kurtosis Kurtosis kurtosis-0.435
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6546000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3bu3a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit

CATH v4.4 (2 domains)

Domain ID domain_id3bu3A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id3bu3A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1

8. Citations (1)

9. Files and Curves (10)