5fpi

Mu2 adaptin subunit of the AP2 adaptor (C-terminal domain) complexed with Integrin alpha4 internalisation peptide QYKSILQE

Method: X-RAY DIFFRACTION Dmax: 87.5 Å Quality: REASONABLE

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 1–435 Fragment:INTERNALISATION SIGNAL BINDING DOMAIN INTEGRIN ALPHA-4 SUBUNIT × 1 (Q8IU71) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;2.2M NACL, 0.4M NAKPHOSPHATE, 20% V/V GLYCEROL, 0.1M MES PH6.5, 5MM DTT Resolution 2.77 Å R-free 0.224

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_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–446; UniProt 1–435

INTEGRIN ALPHA-4 SUBUNIT

OrganismNot specified

UniProt Q8IU71

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 150–157 Fragment:INTERNALISATION SIGNAL PEPTIDE, RESIDUES 150-157 AP-2 COMPLEX SUBUNIT MU × 1 (P84092) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;2.2M NACL, 0.4M NAKPHOSPHATE, 20% V/V GLYCEROL, 0.1M MES PH6.5, 5MM DTT Resolution 2.77 Å R-free 0.224

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q8IU71_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–8; UniProt 150–157

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 5fpi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5fpi
Deposition date deposition_date2015-11-30
Structure title titleMu2 adaptin subunit of the AP2 adaptor (C-terminal domain) complexed with Integrin alpha4 internalisation peptide QYKSILQE
Keywords keywordsENDOCYTOSIS, CLATHRIN ADAPTOR; ENDOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.29
Radius of gyration Rg (electron density) rg_electron23.80
Forward intensity I(0) i014902300.00
Molecular weight molecular_weight30347.0 kDa
Excluded volume excluded_volume38650 ų
Envelope volume envelope_volume48074 ų
Hydration-shell volume shell_volume18389 ų
Envelope diameter envelope_diameter89.2
Shell Rg shell_rg28.63
Envelope Rg envelope_rg24.28
Shape Rg shape_rg23.79
Total Rg total_rg24.51
Total atoms total_atoms2130
Residues n_residues264
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 dmax87.5
Rg (real space) rg_real24.63
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real1.4900e+07
I(0) uncertainty (real space) i0_real_error2.2380e+05
Rg (reciprocal space) rg_reciprocal24.55
I(0) (reciprocal space) i0_reciprocal14900000.0000
Solution quality estimate total_estimate0.5959
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.8
Skewness Skewness skewness0.610
Kurtosis Kurtosis kurtosis-0.215
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5612000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.564; Stabil: 1.000; Sysdev: 0.264; Positv: 1.000; Valcen: 0.392; Smooth: 0.866

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_id5fpiA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B
Domain ID domain_id5fpiA02
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)