1b9k

ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2

Method: X-RAY DIFFRACTION Dmax: 73.7 Å Quality: GOOD

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

PROTEIN (ALPHA-ADAPTIN APPENDAGE DOMAIN)

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 701–938 Fragment:APPENDAGE DOMAIN No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;20% PEG 4000, 10% ISOPROPANOL, 100MM NA CITRATE PH 6.0, 10MM DTT, 6MG/ML PROTEIN Resolution 1.90 Å R-free 0.221

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 1–238; UniProt 701–938

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 1b9k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1b9k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1b9k
Deposition date deposition_date1999-02-11
Structure title titleALPHA-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2
Keywords keywordsENDOCYTOSIS, 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_guinier21.25
Radius of gyration Rg (electron density) rg_electron20.29
Forward intensity I(0) i012365700.00
Molecular weight molecular_weight26627.0 kDa
Excluded volume excluded_volume33514 ų
Envelope volume envelope_volume39426 ų
Hydration-shell volume shell_volume17205 ų
Envelope diameter envelope_diameter73.0
Shell Rg shell_rg25.72
Envelope Rg envelope_rg20.52
Shape Rg shape_rg20.30
Total Rg total_rg21.08
Total atoms total_atoms1875
Residues n_residues237
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 dmax73.7
Rg (real space) rg_real21.35
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.2370e+07
I(0) uncertainty (real space) i0_real_error1.7250e+05
Rg (reciprocal space) rg_reciprocal21.34
I(0) (reciprocal space) i0_reciprocal12370000.0000
Solution quality estimate total_estimate0.8532
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.7
Skewness Skewness skewness0.467
Kurtosis Kurtosis kurtosis-0.287
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3407000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.747; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.852; Smooth: 0.995

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_idd1b9ka1
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_idd1b9ka2
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_id1b9kA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1230 — Gamma-adaptin ear (GAE) domain
Domain ID domain_id1b9kA02
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)