1i31

MU2 ADAPTIN SUBUNIT (AP50) OF AP2 CLATHRIN ADAPTOR, COMPLEXED WITH EGFR INTERNALIZATION PEPTIDE FYRALM AT 2.5 A RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 88.2 Å Quality: GOOD

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

CLATHRIN COAT ASSEMBLY PROTEIN AP50

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 122–435 Fragment:RESIDUES 122-435 EPIDERMAL GROWTH FACTOR RECEPTOR × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;291 K;SODIUM FORMATE, SODIUM ACETATE, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.50 Å R-free 0.255

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 1–314; UniProt 122–435

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 1i31

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1i31
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1i31
Deposition date deposition_date2001-02-12
Structure title titleMU2 ADAPTIN SUBUNIT (AP50) OF AP2 CLATHRIN ADAPTOR, COMPLEXED WITH EGFR INTERNALIZATION PEPTIDE FYRALM AT 2.5 A RESOLUTION
Keywords keywordsbeta-sandwich, peptide-binding site, protein-peptide complex, clathrin adaptor, ENDOCYTOSIS-EXOCYTOSIS COMPLEX; ENDOCYTOSIS/EXOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.22
Radius of gyration Rg (electron density) rg_electron23.73
Forward intensity I(0) i014811200.00
Molecular weight molecular_weight30244.0 kDa
Excluded volume excluded_volume38491 ų
Envelope volume envelope_volume47661 ų
Hydration-shell volume shell_volume18287 ų
Envelope diameter envelope_diameter88.6
Shell Rg shell_rg28.72
Envelope Rg envelope_rg24.27
Shape Rg shape_rg23.72
Total Rg total_rg24.47
Total atoms total_atoms2122
Residues n_residues262
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 dmax88.2
Rg (real space) rg_real24.56
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real1.4810e+07
I(0) uncertainty (real space) i0_real_error2.1310e+05
Rg (reciprocal space) rg_reciprocal24.48
I(0) (reciprocal space) i0_reciprocal14810000.0000
Solution quality estimate total_estimate0.7677
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.7
Skewness Skewness skewness0.614
Kurtosis Kurtosis kurtosis-0.211
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5449000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.539; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.398; Smooth: 0.963

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_idd1i31a_
Class classb — All beta proteins
Fold Fold foldb.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamilyb.2.7 — Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor
Family Family familyb.2.7.1 — Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor

CATH v4.4 (2 domains)

Domain ID domain_id1i31A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B
Domain ID domain_id1i31A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B

8. Citations (2)

9. Files and Curves (10)