2xa7

AP2 clathrin adaptor core in active complex with cargo peptides

Method: X-RAY DIFFRACTION Dmax: 122.3 Å Quality: EXCELLENT

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

ADAPTOR-RELATED PROTEIN COMPLEX 2, ALPHA 2 SUBUNIT

RATTUS NORVEGICUS

UniProt Q66HM2

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–621 Fragment:ALPHA CHAIN, RESIDUES 1-621 AP-2 COMPLEX SUBUNIT BETA × 1 (P63010) AP-2 COMPLEX SUBUNIT MU, × 1 (P84092) TGN38 CARGO PEPTIDE × 1 AP-2 COMPLEX SUBUNIT SIGMA × 1 (P62743) SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.6-0.8M LISO4, 0.6-0.7M NH4SO4, 100MM NA CITRATE PH 6.5; CRYOPROTECTANT 20% GLYCEROL Resolution 3.10 Å R-free 0.285
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–621 Fragment:ALPHA CHAIN, RESIDUES 1-621 AP-2 COMPLEX SUBUNIT BETA × 1 (P63010) AP-2 COMPLEX SUBUNIT MU, × 1 (P84092) AP-2 COMPLEX SUBUNIT SIGMA × 1 (P62743) SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.6-0.8M LISO4, 0.6-0.7M NH4SO4, 100MM NA CITRATE PH 6.5; CRYOPROTECTANT 20% GLYCEROL Resolution 3.10 Å R-free 0.285

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.

8 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q66HM2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–621; UniProt 1–621

AP-2 COMPLEX SUBUNIT BETA

HOMO SAPIENS

UniProt P63010

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–592 Fragment:BETA CHAIN, RESIDUES 1-592 ADAPTOR-RELATED PROTEIN COMPLEX 2, ALPHA 2 SUBUNIT × 1 (Q66HM2) AP-2 COMPLEX SUBUNIT MU, × 1 (P84092) TGN38 CARGO PEPTIDE × 1 AP-2 COMPLEX SUBUNIT SIGMA × 1 (P62743) SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.6-0.8M LISO4, 0.6-0.7M NH4SO4, 100MM NA CITRATE PH 6.5; CRYOPROTECTANT 20% GLYCEROL Resolution 3.10 Å R-free 0.285
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–592 Fragment:BETA CHAIN, RESIDUES 1-592 ADAPTOR-RELATED PROTEIN COMPLEX 2, ALPHA 2 SUBUNIT × 1 (Q66HM2) AP-2 COMPLEX SUBUNIT MU, × 1 (P84092) AP-2 COMPLEX SUBUNIT SIGMA × 1 (P62743) SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.6-0.8M LISO4, 0.6-0.7M NH4SO4, 100MM NA CITRATE PH 6.5; CRYOPROTECTANT 20% GLYCEROL Resolution 3.10 Å R-free 0.285

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.

21 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AP2B1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–592; UniProt 1–592

AP-2 COMPLEX SUBUNIT MU,

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain M; UniProt 1–236 Chain M; UniProt 237–435 Not recorded ADAPTOR-RELATED PROTEIN COMPLEX 2, ALPHA 2 SUBUNIT × 1 (Q66HM2) AP-2 COMPLEX SUBUNIT BETA × 1 (P63010) TGN38 CARGO PEPTIDE × 1 AP-2 COMPLEX SUBUNIT SIGMA × 1 (P62743) SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.6-0.8M LISO4, 0.6-0.7M NH4SO4, 100MM NA CITRATE PH 6.5; CRYOPROTECTANT 20% GLYCEROL Resolution 3.10 Å R-free 0.285
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain M; UniProt 1–236 Chain M; UniProt 237–435 Not recorded ADAPTOR-RELATED PROTEIN COMPLEX 2, ALPHA 2 SUBUNIT × 1 (Q66HM2) AP-2 COMPLEX SUBUNIT BETA × 1 (P63010) AP-2 COMPLEX SUBUNIT SIGMA × 1 (P62743) SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.6-0.8M LISO4, 0.6-0.7M NH4SO4, 100MM NA CITRATE PH 6.5; CRYOPROTECTANT 20% GLYCEROL Resolution 3.10 Å R-free 0.285

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 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AP2M1_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain M; PDBConstruct 1–236; UniProt 1–236 Author chain M; PDBConstruct 248–446; UniProt 237–435

AP-2 COMPLEX SUBUNIT SIGMA

MUS MUSCULUS

UniProt P62743

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain S; UniProt 1–142 Not recorded ADAPTOR-RELATED PROTEIN COMPLEX 2, ALPHA 2 SUBUNIT × 1 (Q66HM2) AP-2 COMPLEX SUBUNIT BETA × 1 (P63010) AP-2 COMPLEX SUBUNIT MU, × 1 (P84092) TGN38 CARGO PEPTIDE × 1 SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.6-0.8M LISO4, 0.6-0.7M NH4SO4, 100MM NA CITRATE PH 6.5; CRYOPROTECTANT 20% GLYCEROL Resolution 3.10 Å R-free 0.285
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain S; UniProt 1–142 Not recorded ADAPTOR-RELATED PROTEIN COMPLEX 2, ALPHA 2 SUBUNIT × 1 (Q66HM2) AP-2 COMPLEX SUBUNIT BETA × 1 (P63010) AP-2 COMPLEX SUBUNIT MU, × 1 (P84092) SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.6-0.8M LISO4, 0.6-0.7M NH4SO4, 100MM NA CITRATE PH 6.5; CRYOPROTECTANT 20% GLYCEROL Resolution 3.10 Å R-free 0.285

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.

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

View Construct and Data Evidence
UniProt name AP2S1_MOUSE
Isoform
PDB entities 5
Chains and sequence ranges Author chain S; PDBConstruct 1–142; UniProt 1–142

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 2xa7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2xa7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2xa7
Deposition date deposition_date2010-03-29
Structure title titleAP2 clathrin adaptor core in active complex with cargo peptides
Keywords keywordsPHOSPHOPROTEIN, PROTEIN TRANSPORT, ENDOCYTOSIS, CELL MEMBRANE, LIPID-BINDING; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.06
Radius of gyration Rg (electron density) rg_electron39.29
Forward intensity I(0) i0575159000.00
Molecular weight molecular_weight201230.0 kDa
Excluded volume excluded_volume254300 ų
Envelope volume envelope_volume346340 ų
Hydration-shell volume shell_volume70778 ų
Envelope diameter envelope_diameter131.5
Shell Rg shell_rg47.39
Envelope Rg envelope_rg38.46
Shape Rg shape_rg39.27
Total Rg total_rg39.81
Total atoms total_atoms14137
Residues n_residues1768
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 dmax122.3
Rg (real space) rg_real39.84
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real5.7520e+08
I(0) uncertainty (real space) i0_real_error9.4690e+06
Rg (reciprocal space) rg_reciprocal40.05
I(0) (reciprocal space) i0_reciprocal575300000.0000
Solution quality estimate total_estimate0.9030
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary56.5
Skewness Skewness skewness0.043
Kurtosis Kurtosis kurtosis-0.591
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha137300000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.930

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id2xa7A01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id2xa7B00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id2xa7M01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily60
Domain ID domain_id2xa7S00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily60

8. Citations (1)

9. Files and Curves (10)