6qh5

AP2 clathrin adaptor mu2T156-phosphorylated core in closed conformation

Method: X-RAY DIFFRACTION Dmax: 124.2 Å Quality: EXCELLENT

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

AP-2 complex subunit alpha

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 Not recorded AP-2 complex subunit beta × 1 (P63010) AP-2 complex subunit mu × 1 (P84092) AP-2 complex subunit mu × 1 (P84092) AP-2 complex subunit sigma × 1 (P62743) IHP INOSITOL HEXAKISPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;289 K;20% PEG 1000; 100 mM Na+/K+ phosphate buffer (pH 7.2), 200 mM NaCl, and 10 mM DTT Resolution 2.56 Å R-free 0.257

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 12 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 Not recorded AP-2 complex subunit alpha × 1 (Q66HM2) AP-2 complex subunit mu × 1 (P84092) AP-2 complex subunit mu × 1 (P84092) AP-2 complex subunit sigma × 1 (P62743) IHP INOSITOL HEXAKISPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;289 K;20% PEG 1000; 100 mM Na+/K+ phosphate buffer (pH 7.2), 200 mM NaCl, and 10 mM DTT Resolution 2.56 Å R-free 0.257

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 25 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 1–435 Chain N; UniProt 1–435 Non-standard monomer:Yes (specific site not provided by mmCIF) AP-2 complex subunit alpha × 1 (Q66HM2) AP-2 complex subunit beta × 1 (P63010) AP-2 complex subunit sigma × 1 (P62743) IHP INOSITOL HEXAKISPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;289 K;20% PEG 1000; 100 mM Na+/K+ phosphate buffer (pH 7.2), 200 mM NaCl, and 10 mM DTT Resolution 2.56 Å R-free 0.257

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 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AP2M1_RAT
Isoform
PDB entities 3, 4
Chains and sequence ranges Author chain N; PDBConstruct 1–446; UniProt 1–435 Author chain M; PDBConstruct 1–446; UniProt 1–435

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 AP-2 complex subunit alpha × 1 (Q66HM2) AP-2 complex subunit beta × 1 (P63010) AP-2 complex subunit mu × 1 (P84092) AP-2 complex subunit mu × 1 (P84092) IHP INOSITOL HEXAKISPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;289 K;20% PEG 1000; 100 mM Na+/K+ phosphate buffer (pH 7.2), 200 mM NaCl, and 10 mM DTT Resolution 2.56 Å R-free 0.257

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 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 6qh5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6qh5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6qh5
Deposition date deposition_date2019-01-15
Structure title titleAP2 clathrin adaptor mu2T156-phosphorylated core in closed conformation
Keywords keywordsENDOCYTOSIS, PHOSPHORYLATION, CELL MEMBRANE, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.73
Radius of gyration Rg (electron density) rg_electron38.78
Forward intensity I(0) i0542350000.00
Molecular weight molecular_weight195640.0 kDa
Excluded volume excluded_volume247360 ų
Envelope volume envelope_volume325740 ų
Hydration-shell volume shell_volume67839 ų
Envelope diameter envelope_diameter124.0
Shell Rg shell_rg46.59
Envelope Rg envelope_rg38.00
Shape Rg shape_rg38.75
Total Rg total_rg39.31
Total atoms total_atoms13743
Residues n_residues1717
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 dmax124.2
Rg (real space) rg_real39.46
Rg uncertainty (real space) rg_real_error1.07
I(0) (real space) i0_real5.4240e+08
I(0) uncertainty (real space) i0_real_error9.5500e+06
Rg (reciprocal space) rg_reciprocal39.63
I(0) (reciprocal space) i0_reciprocal542400000.0000
Solution quality estimate total_estimate0.9038
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.8
Skewness Skewness skewness0.103
Kurtosis Kurtosis kurtosis-0.587
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha128000000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.948

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd6qh5a_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.10 — Clathrin adaptor core protein
Domain ID domain_idd6qh5b_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.10 — Clathrin adaptor core protein
Domain ID domain_idd6qh5n_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.110 — Profilin-like
Superfamily Superfamily superfamilyd.110.4 — SNARE-like
Family Family familyd.110.4.2 — Clathrin coat assembly domain
Domain ID domain_idd6qh5s_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.110 — Profilin-like
Superfamily Superfamily superfamilyd.110.4 — SNARE-like
Family Family familyd.110.4.2 — Clathrin coat assembly domain

CATH v4.4 (6 domains)

Domain ID domain_id6qh5A00
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_id6qh5B00
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_id6qh5M01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B
Domain ID domain_id6qh5M02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B
Domain ID domain_id6qh5N00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily60
Domain ID domain_id6qh5S00
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)