2vgl

AP2 CLATHRIN ADAPTOR CORE

Method: X-RAY DIFFRACTION Dmax: 123.2 Å Quality: EXCELLENT

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

ADAPTOR PROTEIN COMPLEX AP-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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–621 Fragment:1-621 AP-2 COMPLEX SUBUNIT BETA-1 × 1 (P63010) AP-2 COMPLEX SUBUNIT MU-1 × 1 (P84092) AP-2 COMPLEX SUBUNIT SIGMA-1 × 1 (P62743) IHP INOSITOL HEXAKISPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.2;18% PEG, 10MM NA/K PHOSPHATE PH 6.2, 200MM NACL, 4MM DTT, IP6 Resolution 2.60 Å R-free 0.339

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-1

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–591 Fragment:1-591 ADAPTOR PROTEIN COMPLEX AP-2, ALPHA 2 SUBUNIT × 1 (Q66HM2) AP-2 COMPLEX SUBUNIT MU-1 × 1 (P84092) AP-2 COMPLEX SUBUNIT SIGMA-1 × 1 (P62743) IHP INOSITOL HEXAKISPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.2;18% PEG, 10MM NA/K PHOSPHATE PH 6.2, 200MM NACL, 4MM DTT, IP6 Resolution 2.60 Å R-free 0.339

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 1–591; UniProt 1–591

AP-2 COMPLEX SUBUNIT MU-1

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain M; UniProt 1–435 Not recorded ADAPTOR PROTEIN COMPLEX AP-2, ALPHA 2 SUBUNIT × 1 (Q66HM2) AP-2 COMPLEX SUBUNIT BETA-1 × 1 (P63010) AP-2 COMPLEX SUBUNIT SIGMA-1 × 1 (P62743) IHP INOSITOL HEXAKISPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.2;18% PEG, 10MM NA/K PHOSPHATE PH 6.2, 200MM NACL, 4MM DTT, IP6 Resolution 2.60 Å R-free 0.339

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
Chains and sequence ranges Author chain M; PDBConstruct 1–435; UniProt 1–435

AP-2 COMPLEX SUBUNIT SIGMA-1

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain S; UniProt 1–142 Not recorded ADAPTOR PROTEIN COMPLEX AP-2, ALPHA 2 SUBUNIT × 1 (Q66HM2) AP-2 COMPLEX SUBUNIT BETA-1 × 1 (P63010) AP-2 COMPLEX SUBUNIT MU-1 × 1 (P84092) IHP INOSITOL HEXAKISPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.2;18% PEG, 10MM NA/K PHOSPHATE PH 6.2, 200MM NACL, 4MM DTT, IP6 Resolution 2.60 Å R-free 0.339

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 4
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 2vgl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2vgl
Deposition date deposition_date2007-11-14
Structure title titleAP2 CLATHRIN ADAPTOR CORE
Keywords keywords;CYTOPLASMIC VESICLE, ALTERNATIVE SPLICING, ENDOCYTOSIS, LIPID-BINDING, GOLGI APPARATUS, ADAPTOR, MEMBRANE, TRANSPORT, COATED PIT, PHOSPHORYLATION, 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_guinier39.74
Radius of gyration Rg (electron density) rg_electron38.79
Forward intensity I(0) i0542464000.00
Molecular weight molecular_weight195630.0 kDa
Excluded volume excluded_volume247360 ų
Envelope volume envelope_volume325440 ų
Hydration-shell volume shell_volume67787 ų
Envelope diameter envelope_diameter124.6
Shell Rg shell_rg46.54
Envelope Rg envelope_rg38.03
Shape Rg shape_rg38.77
Total Rg total_rg39.32
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 dmax123.2
Rg (real space) rg_real39.47
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real5.4250e+08
I(0) uncertainty (real space) i0_real_error9.9520e+06
Rg (reciprocal space) rg_reciprocal39.64
I(0) (reciprocal space) i0_reciprocal542600000.0000
Solution quality estimate total_estimate0.9040
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.4
Skewness Skewness skewness0.103
Kurtosis Kurtosis kurtosis-0.586
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha127800000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.931

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_idd2vgla_
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_idd2vglb_
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_idd2vglm1
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_idd2vgls_
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_id2vglA00
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_id2vglB00
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_id2vglM01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily60
Domain ID domain_id2vglM02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B
Domain ID domain_id2vglM03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B
Domain ID domain_id2vglS00
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)