2vj0

Crystal structure of the alpha-adaptin appendage domain, from the AP2 adaptor complex, in complex with an FXDNF peptide from amphiphysin1 and a WVXF peptide from synaptojanin P170

Method: X-RAY DIFFRACTION Dmax: 71.5 Å Quality: GOOD

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

AP-2 COMPLEX SUBUNIT ALPHA-2

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 693–938 Fragment:APPENDAGE DOMAIN, RESIDUES 693-938 SYNAPTOJANIN-1 × 1 (O43426) AMPHIPHYSIN × 1 (O08838) BEN BENZAMIDINE × 1 DTD DITHIANE DIOL × 1 SO4 SULFATE ION × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;1.2M AMMONIUM SULPHATE, 3% ISOPROPANOL AND 0.05M SODIUM CITRATE PH 6.5 Resolution 1.60 Å R-free 0.208

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 5–250; UniProt 693–938

SYNAPTOJANIN-1

OrganismNot specified

UniProt O43426

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain P; UniProt 1479–1490 Fragment:PEPTIDE CONTAINING WVXF MOTIF, RESIDUES 1479-1490 AP-2 COMPLEX SUBUNIT ALPHA-2 × 1 (P17427) AMPHIPHYSIN × 1 (O08838) BEN BENZAMIDINE × 1 DTD DITHIANE DIOL × 1 SO4 SULFATE ION × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;1.2M AMMONIUM SULPHATE, 3% ISOPROPANOL AND 0.05M SODIUM CITRATE PH 6.5 Resolution 1.60 Å R-free 0.208

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.

4 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYNJ1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–12; UniProt 1479–1490

AMPHIPHYSIN

OrganismNot specified

UniProt O08838

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain Q; UniProt 324–330 Fragment:PEPTIDE CONTAINING FXDNF MOTIF, RESIDUES 324-330 AP-2 COMPLEX SUBUNIT ALPHA-2 × 1 (P17427) SYNAPTOJANIN-1 × 1 (O43426) BEN BENZAMIDINE × 1 DTD DITHIANE DIOL × 1 SO4 SULFATE ION × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;1.2M AMMONIUM SULPHATE, 3% ISOPROPANOL AND 0.05M SODIUM CITRATE PH 6.5 Resolution 1.60 Å R-free 0.208

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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AMPH_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain Q; PDBConstruct 1–7; UniProt 324–330

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 2vj0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2vj0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2vj0
Deposition date deposition_date2007-12-06
Structure title titleCrystal structure of the alpha-adaptin appendage domain, from the AP2 adaptor complex, in complex with an FXDNF peptide from amphiphysin1 and a WVXF peptide from synaptojanin P170
Keywords keywords;PROTEIN TRANSPORT, CYTOPLASMIC VESICLE, ALTERNATIVE SPLICING, TRANSPORT, COATED PIT, SH3 DOMAIN, ENDOCYTOSIS, ALPHA-ADAPTIN, GOLGI APPARATUS, PHOSPHORYLATION, AP2, SYNAPSE, MEMBRANE, CYTOPLASM, COILED COIL, AMPHIPHYSIN, CYTOSKELETON, SYNAPTOJANIN, LIPID-BINDING, CELL JUNCTION ;; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.35
Radius of gyration Rg (electron density) rg_electron20.41
Forward intensity I(0) i015735900.00
Molecular weight molecular_weight29926.0 kDa
Excluded volume excluded_volume37483 ų
Envelope volume envelope_volume43704 ų
Hydration-shell volume shell_volume18647 ų
Envelope diameter envelope_diameter70.9
Shell Rg shell_rg26.07
Envelope Rg envelope_rg20.65
Shape Rg shape_rg20.43
Total Rg total_rg21.16
Total atoms total_atoms2101
Residues n_residues261
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 dmax71.5
Rg (real space) rg_real21.43
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.5740e+07
I(0) uncertainty (real space) i0_real_error2.2380e+05
Rg (reciprocal space) rg_reciprocal21.41
I(0) (reciprocal space) i0_reciprocal15740000.0000
Solution quality estimate total_estimate0.8716
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.1
Skewness Skewness skewness0.472
Kurtosis Kurtosis kurtosis-0.201
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3313000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.806; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.949; Smooth: 0.961

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2vj0a1
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_idd2vj0a2
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_id2vj0A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1230 — Gamma-adaptin ear (GAE) domain
Domain ID domain_id2vj0A02
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)