1qts

CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE

Method: X-RAY DIFFRACTION Dmax: 72.2 Å Quality: GOOD

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

AP-2 CLATHRIN ADAPTOR ALPHA SUBUNIT (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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 692–938 Fragment:C-TERMINAL APPENDAGE (EAR) RESIDUES 701-938 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.9;293 K;1.3 M AMMONIUM SULFATE, 80 MM HEPES, 8% DIOXANE, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.40 Å R-free 0.209

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 1–247; UniProt 692–938

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 1qts

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1qts
Deposition date deposition_date1999-06-29
Structure title titleCRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE
Keywords keywordsMEMBRANE PROTEIN, FOUR-WAVELENGTH MAD, SELENOMETHIONINE; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.05
Radius of gyration Rg (electron density) rg_electron20.10
Forward intensity I(0) i013646800.00
Molecular weight molecular_weight27804.0 kDa
Excluded volume excluded_volume34911 ų
Envelope volume envelope_volume41066 ų
Hydration-shell volume shell_volume17962 ų
Envelope diameter envelope_diameter72.2
Shell Rg shell_rg25.53
Envelope Rg envelope_rg20.24
Shape Rg shape_rg20.11
Total Rg total_rg20.87
Total atoms total_atoms1957
Residues n_residues247
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 dmax72.2
Rg (real space) rg_real21.11
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real1.3650e+07
I(0) uncertainty (real space) i0_real_error2.0410e+05
Rg (reciprocal space) rg_reciprocal21.10
I(0) (reciprocal space) i0_reciprocal13650000.0000
Solution quality estimate total_estimate0.8640
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.459
Kurtosis Kurtosis kurtosis-0.184
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2904000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.772; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.944; Smooth: 0.970

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1qtsa1
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_idd1qtsa2
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

CATH v4.4 (2 domains)

Domain ID domain_id1qtsA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1230 — Gamma-adaptin ear (GAE) domain
Domain ID domain_id1qtsA02
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)