2jkt

AP2 CLATHRIN ADAPTOR CORE with CD4 Dileucine peptide RM(phosphoS) EIKRLLSE Q to E mutant

Method: X-RAY DIFFRACTION Dmax: 177.6 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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–271 Chain A; UniProt 272–620 Fragment:ALPHA CHAIN, RESIDUES 1-620 AP-2 COMPLEX SUBUNIT BETA-1 × 1 (P63010) AP-2 COMPLEX SUBUNIT SIGMA-1 × 1 (P62743) AP-2 COMPLEX SUBUNIT MU-1 × 1 (P84092) CD4 PEPTIDE × 1 (B0AZV7) SO4 SULFATE ION × 15 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;1.7-2.2M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH6 .5 AND 5MM DTT FROM A MIXTURE OF 10MG/ML AP2 CORE AND 7MG/ML PEPTIDE. CRYOPROTECTED WITH 1.8-2.3M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH 6.5, 17% GLYCEROL AND 7MG/ ML CD4 DILEUCINE PEPTIDE Resolution 3.40 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain L; UniProt 1–271 Chain L; UniProt 272–620 Fragment:ALPHA CHAIN, RESIDUES 1-620 AP-2 COMPLEX SUBUNIT BETA-1 × 1 (P63010) AP-2 COMPLEX SUBUNIT SIGMA-1 × 1 (P62743) AP-2 COMPLEX SUBUNIT MU-1 × 1 (P84092) CD4 PEPTIDE × 1 (B0AZV7) SO4 SULFATE ION × 16 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;1.7-2.2M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH6 .5 AND 5MM DTT FROM A MIXTURE OF 10MG/ML AP2 CORE AND 7MG/ML PEPTIDE. CRYOPROTECTED WITH 1.8-2.3M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH 6.5, 17% GLYCEROL AND 7MG/ ML CD4 DILEUCINE PEPTIDE Resolution 3.40 Å R-free 0.256

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 25 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 1–271; UniProt 1–271 Author chain A; PDBConstruct 273–621; UniProt 272–620 Author chain L; PDBConstruct 1–271; UniProt 1–271 Author chain L; PDBConstruct 273–621; UniProt 272–620

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–591 Fragment:BETA2 CHAIN, RESIDUES 1-591 AP-2 COMPLEX SUBUNIT ALPHA-2 × 1 (P17427) AP-2 COMPLEX SUBUNIT SIGMA-1 × 1 (P62743) AP-2 COMPLEX SUBUNIT MU-1 × 1 (P84092) CD4 PEPTIDE × 1 (B0AZV7) SO4 SULFATE ION × 15 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;1.7-2.2M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH6 .5 AND 5MM DTT FROM A MIXTURE OF 10MG/ML AP2 CORE AND 7MG/ML PEPTIDE. CRYOPROTECTED WITH 1.8-2.3M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH 6.5, 17% GLYCEROL AND 7MG/ ML CD4 DILEUCINE PEPTIDE Resolution 3.40 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–591 Fragment:BETA2 CHAIN, RESIDUES 1-591 AP-2 COMPLEX SUBUNIT ALPHA-2 × 1 (P17427) AP-2 COMPLEX SUBUNIT SIGMA-1 × 1 (P62743) AP-2 COMPLEX SUBUNIT MU-1 × 1 (P84092) CD4 PEPTIDE × 1 (B0AZV7) SO4 SULFATE ION × 16 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;1.7-2.2M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH6 .5 AND 5MM DTT FROM A MIXTURE OF 10MG/ML AP2 CORE AND 7MG/ML PEPTIDE. CRYOPROTECTED WITH 1.8-2.3M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH 6.5, 17% GLYCEROL AND 7MG/ ML CD4 DILEUCINE PEPTIDE Resolution 3.40 Å R-free 0.256

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 1–591; UniProt 1–591 Author chain E; PDBConstruct 1–591; UniProt 1–591

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain S; UniProt 1–142 Not recorded AP-2 COMPLEX SUBUNIT ALPHA-2 × 1 (P17427) AP-2 COMPLEX SUBUNIT BETA-1 × 1 (P63010) AP-2 COMPLEX SUBUNIT MU-1 × 1 (P84092) CD4 PEPTIDE × 1 (B0AZV7) SO4 SULFATE ION × 15 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;1.7-2.2M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH6 .5 AND 5MM DTT FROM A MIXTURE OF 10MG/ML AP2 CORE AND 7MG/ML PEPTIDE. CRYOPROTECTED WITH 1.8-2.3M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH 6.5, 17% GLYCEROL AND 7MG/ ML CD4 DILEUCINE PEPTIDE Resolution 3.40 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain I; UniProt 1–142 Not recorded AP-2 COMPLEX SUBUNIT ALPHA-2 × 1 (P17427) AP-2 COMPLEX SUBUNIT BETA-1 × 1 (P63010) AP-2 COMPLEX SUBUNIT MU-1 × 1 (P84092) CD4 PEPTIDE × 1 (B0AZV7) SO4 SULFATE ION × 16 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;1.7-2.2M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH6 .5 AND 5MM DTT FROM A MIXTURE OF 10MG/ML AP2 CORE AND 7MG/ML PEPTIDE. CRYOPROTECTED WITH 1.8-2.3M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH 6.5, 17% GLYCEROL AND 7MG/ ML CD4 DILEUCINE PEPTIDE Resolution 3.40 Å R-free 0.256

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 3
Chains and sequence ranges Author chain I; PDBConstruct 1–142; UniProt 1–142 Author chain S; PDBConstruct 1–142; UniProt 1–142

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain M; UniProt 1–435 Not recorded AP-2 COMPLEX SUBUNIT ALPHA-2 × 1 (P17427) AP-2 COMPLEX SUBUNIT BETA-1 × 1 (P63010) AP-2 COMPLEX SUBUNIT SIGMA-1 × 1 (P62743) CD4 PEPTIDE × 1 (B0AZV7) SO4 SULFATE ION × 15 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;1.7-2.2M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH6 .5 AND 5MM DTT FROM A MIXTURE OF 10MG/ML AP2 CORE AND 7MG/ML PEPTIDE. CRYOPROTECTED WITH 1.8-2.3M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH 6.5, 17% GLYCEROL AND 7MG/ ML CD4 DILEUCINE PEPTIDE Resolution 3.40 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain U; UniProt 1–435 Not recorded AP-2 COMPLEX SUBUNIT ALPHA-2 × 1 (P17427) AP-2 COMPLEX SUBUNIT BETA-1 × 1 (P63010) AP-2 COMPLEX SUBUNIT SIGMA-1 × 1 (P62743) CD4 PEPTIDE × 1 (B0AZV7) SO4 SULFATE ION × 16 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;1.7-2.2M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH6 .5 AND 5MM DTT FROM A MIXTURE OF 10MG/ML AP2 CORE AND 7MG/ML PEPTIDE. CRYOPROTECTED WITH 1.8-2.3M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH 6.5, 17% GLYCEROL AND 7MG/ ML CD4 DILEUCINE PEPTIDE Resolution 3.40 Å R-free 0.256

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 4
Chains and sequence ranges Author chain M; PDBConstruct 1–435; UniProt 1–435 Author chain U; PDBConstruct 1–435; UniProt 1–435

CD4 PEPTIDE

OrganismNot specified

UniProt B0AZV7

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 P; UniProt 252–262 Fragment:RESIDUES 252-262 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) AP-2 COMPLEX SUBUNIT ALPHA-2 × 1 (P17427) AP-2 COMPLEX SUBUNIT BETA-1 × 1 (P63010) AP-2 COMPLEX SUBUNIT SIGMA-1 × 1 (P62743) AP-2 COMPLEX SUBUNIT MU-1 × 1 (P84092) SO4 SULFATE ION × 15 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;1.7-2.2M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH6 .5 AND 5MM DTT FROM A MIXTURE OF 10MG/ML AP2 CORE AND 7MG/ML PEPTIDE. CRYOPROTECTED WITH 1.8-2.3M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH 6.5, 17% GLYCEROL AND 7MG/ ML CD4 DILEUCINE PEPTIDE Resolution 3.40 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain Q; UniProt 252–262 Fragment:RESIDUES 252-262 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) AP-2 COMPLEX SUBUNIT ALPHA-2 × 1 (P17427) AP-2 COMPLEX SUBUNIT BETA-1 × 1 (P63010) AP-2 COMPLEX SUBUNIT SIGMA-1 × 1 (P62743) AP-2 COMPLEX SUBUNIT MU-1 × 1 (P84092) SO4 SULFATE ION × 16 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;1.7-2.2M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH6 .5 AND 5MM DTT FROM A MIXTURE OF 10MG/ML AP2 CORE AND 7MG/ML PEPTIDE. CRYOPROTECTED WITH 1.8-2.3M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH 6.5, 17% GLYCEROL AND 7MG/ ML CD4 DILEUCINE PEPTIDE Resolution 3.40 Å R-free 0.256

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 B0AZV7_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain P; PDBConstruct 1–11; UniProt 252–262 Author chain Q; PDBConstruct 1–11; UniProt 252–262

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 2jkt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2jkt
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2jkt
Deposition date deposition_date2008-08-29
Structure title titleAP2 CLATHRIN ADAPTOR CORE with CD4 Dileucine peptide RM(phosphoS) EIKRLLSE Q to E mutant
Keywords keywords;ALTERNATIVE SPLICING, PHOSPHOPROTEIN, PHOSPHORYLATION, PROTEIN TRANSPORT, ADAPTOR, MEMBRANE, TRANSPORT, COATED PIT, ENDOCYTOSIS, CELL MEMBRANE, LIPID-BINDING ;; ENDOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier57.27
Radius of gyration Rg (electron density) rg_electron57.41
Forward intensity I(0) i02191660000.00
Molecular weight molecular_weight400610.0 kDa
Excluded volume excluded_volume505200 ų
Envelope volume envelope_volume709110 ų
Hydration-shell volume shell_volume104200 ų
Envelope diameter envelope_diameter194.1
Shell Rg shell_rg57.88
Envelope Rg envelope_rg56.61
Shape Rg shape_rg57.37
Total Rg total_rg57.54
Total atoms total_atoms28101
Residues n_residues3502
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 dmax177.6
Rg (real space) rg_real57.50
Rg uncertainty (real space) rg_real_error1.72
I(0) (real space) i0_real2.1920e+09
I(0) uncertainty (real space) i0_real_error4.5140e+07
Rg (reciprocal space) rg_reciprocal57.06
I(0) (reciprocal space) i0_reciprocal2190000000.0000
Solution quality estimate total_estimate0.8333
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary65.8
Skewness Skewness skewness0.448
Kurtosis Kurtosis kurtosis-0.367
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha159900000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.015

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id2jktA01
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_id2jktB00
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_id2jktE00
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_id2jktI00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily60
Domain ID domain_id2jktL01
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_id2jktM01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily60
Domain ID domain_id2jktM02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B
Domain ID domain_id2jktM03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B
Domain ID domain_id2jktS00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily60
Domain ID domain_id2jktU01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily60
Domain ID domain_id2jktU02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B
Domain ID domain_id2jktU03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B

8. Citations (1)

9. Files and Curves (10)