5wrk

Mu2 subunit of the clathrin adaptor complex AP2 in complex with IRS-1 Y608 peptide

Method: X-RAY DIFFRACTION Dmax: 86.4 Å Quality: GOOD

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

AP-2 complex subunit mu

Rattus norvegicus

UniProt P84092

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 158–223 Chain A; UniProt 261–435 Fragment:UNP residues 158-223,UNP residues 261-435 Insulin receptor substrate 1 × 1 (P35570) NI NICKEL (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.4M Na formate, 0.05M NiCl, 0.1M Na acetate pH 6.0 Resolution 2.62 Å R-free 0.223

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.

35 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AP2M1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–66; UniProt 158–223 Author chain A; PDBConstruct 104–278; UniProt 261–435

Insulin receptor substrate 1

OrganismNot specified

UniProt P35570

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 607–614 Not recorded AP-2 complex subunit mu × 1 (P84092) NI NICKEL (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.4M Na formate, 0.05M NiCl, 0.1M Na acetate pH 6.0 Resolution 2.62 Å R-free 0.223

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 IRS1_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–8; UniProt 607–614

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 5wrk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5wrk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5wrk
Deposition date deposition_date2016-12-02
Structure title titleMu2 subunit of the clathrin adaptor complex AP2 in complex with IRS-1 Y608 peptide
Keywords keywordsEndocytosis, clathrin adaptor AP-2 complex subunit, peptide complex; ENDOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.19
Radius of gyration Rg (electron density) rg_electron23.72
Forward intensity I(0) i013422700.00
Molecular weight molecular_weight28657.0 kDa
Excluded volume excluded_volume36450 ų
Envelope volume envelope_volume44822 ų
Hydration-shell volume shell_volume17482 ų
Envelope diameter envelope_diameter88.9
Shell Rg shell_rg28.30
Envelope Rg envelope_rg24.04
Shape Rg shape_rg23.70
Total Rg total_rg24.44
Total atoms total_atoms2005
Residues n_residues251
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 dmax86.4
Rg (real space) rg_real24.55
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real1.3420e+07
I(0) uncertainty (real space) i0_real_error1.9700e+05
Rg (reciprocal space) rg_reciprocal24.47
I(0) (reciprocal space) i0_reciprocal13420000.0000
Solution quality estimate total_estimate0.7668
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.2
Skewness Skewness skewness0.614
Kurtosis Kurtosis kurtosis-0.235
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5346000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.563; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.406; Smooth: 0.868

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5wrkA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B
Domain ID domain_id5wrkA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B

8. Citations (1)

9. Files and Curves (10)