1kyf

AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPS15 DPF PEPTIDE

Method: X-RAY DIFFRACTION Dmax: 73.3 Å Quality: REASONABLE

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

ALPHA-ADAPTIN C

Mus musculus

UniProt P17427

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 701–938 Fragment:C-TERMINAL APPENDAGE (EAR) RESIDUES 701-938 Epidermal growth factor receptor substrate 15 × 1 (P42567) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.22 Å R-free 0.211

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.

23 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AP2A2_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 10–247; UniProt 701–938

Epidermal growth factor receptor substrate 15

OrganismNot specified

UniProt P42567

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 627–632 Fragment:RESIDUES 628-632 ALPHA-ADAPTIN C × 1 (P17427) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.22 Å R-free 0.211

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 EP15_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–6; UniProt 627–632

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 1kyf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1kyf
Deposition date deposition_date2002-02-04
Structure title titleAP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPS15 DPF PEPTIDE
Keywords keywordsPROTEIN-PEPTIDE COMPLEX, ENDOCYTOSIS, 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_guinier21.26
Radius of gyration Rg (electron density) rg_electron20.34
Forward intensity I(0) i014191200.00
Molecular weight molecular_weight28396.0 kDa
Excluded volume excluded_volume35657 ų
Envelope volume envelope_volume42310 ų
Hydration-shell volume shell_volume18264 ų
Envelope diameter envelope_diameter74.1
Shell Rg shell_rg25.84
Envelope Rg envelope_rg20.56
Shape Rg shape_rg20.35
Total Rg total_rg21.11
Total atoms total_atoms3896
Residues n_residues252
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 dmax73.3
Rg (real space) rg_real21.35
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real1.4190e+07
I(0) uncertainty (real space) i0_real_error1.8670e+05
Rg (reciprocal space) rg_reciprocal21.33
I(0) (reciprocal space) i0_reciprocal14190000.0000
Solution quality estimate total_estimate0.6026
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.6
Skewness Skewness skewness0.493
Kurtosis Kurtosis kurtosis-0.122
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3307000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.749; Stabil: 1.000; Sysdev: 0.225; Positv: 1.000; Valcen: 0.910; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1kyfa1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.10 — Clathrin adaptor appendage domain
Family Family familyb.1.10.1 — Alpha-adaptin ear subdomain-like
Domain ID domain_idd1kyfa2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.105 — Subdomain of clathrin and coatomer appendage domain
Superfamily Superfamily superfamilyd.105.1 — Subdomain of clathrin and coatomer appendage domain
Family Family familyd.105.1.1 — Clathrin adaptor appendage, alpha and beta chain-specific domain
Domain ID domain_idd1kyfa3
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_id1kyfA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1230 — Gamma-adaptin ear (GAE) domain
Domain ID domain_id1kyfA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology310 — TATA-Binding Protein
Homologous superfamily homologous superfamily10 — TATA-Binding Protein

8. Citations (1)

9. Files and Curves (10)