2iv9

B2-appendage from AP2 in complex with Eps15 peptide

Method: X-RAY DIFFRACTION Dmax: 92.3 Å Quality: GOOD

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

AP-2 COMPLEX SUBUNIT BETA-2

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 700–937 Chain B; UniProt 700–937 Fragment:APPENDAGE DOMAIN, RESIDUES 700-937 EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15 ISOFORM B × 1 (Q5JC29) SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.5;2M AMMONIUM SULPHATE, 0.1M AMMONIUM ACETATE PH 4.5 Resolution 1.90 Å R-free 0.267

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–238; UniProt 700–937 Author chain B; PDBConstruct 1–238; UniProt 700–937

EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15 ISOFORM B

OrganismNot specified

UniProt Q5JC29

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 720–731 Fragment:RESIDUES 720-731 AP-2 COMPLEX SUBUNIT BETA-2 × 2 (P63010) SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.5;2M AMMONIUM SULPHATE, 0.1M AMMONIUM ACETATE PH 4.5 Resolution 1.90 Å R-free 0.267

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q5JC29_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–12; UniProt 720–731

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 2iv9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2iv9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2iv9
Deposition date deposition_date2006-06-08
Structure title titleB2-appendage from AP2 in complex with Eps15 peptide
Keywords keywords;ENDOCYTOSIS/REGULATOR, ALTERNATIVE SPLICING, ENDOCYTOSIS-REGULATOR COMPLEX, B2, EAR, EPS15, ADAPTOR, CALCIUM, APPENDAGE, COATED PITS, ENDOCYTOSIS, PHOSPHORYLATION ;; ENDOCYTOSIS/REGULATOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.91
Radius of gyration Rg (electron density) rg_electron25.87
Forward intensity I(0) i046141700.00
Molecular weight molecular_weight54080.0 kDa
Excluded volume excluded_volume68242 ų
Envelope volume envelope_volume83571 ų
Hydration-shell volume shell_volume27485 ų
Envelope diameter envelope_diameter96.2
Shell Rg shell_rg32.34
Envelope Rg envelope_rg25.98
Shape Rg shape_rg25.85
Total Rg total_rg26.63
Total atoms total_atoms3801
Residues n_residues478
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 dmax92.3
Rg (real space) rg_real26.91
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real4.6140e+07
I(0) uncertainty (real space) i0_real_error6.3810e+05
Rg (reciprocal space) rg_reciprocal26.91
I(0) (reciprocal space) i0_reciprocal46140000.0000
Solution quality estimate total_estimate0.8784
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.7
Skewness Skewness skewness0.327
Kurtosis Kurtosis kurtosis-0.322
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9580000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.836; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.924; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2iv9a1
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_idd2iv9a2
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
Domain ID domain_idd2iv9b1
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_idd2iv9b2
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 (4 domains)

Domain ID domain_id2iv9A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1150
Domain ID domain_id2iv9A02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology310 — TATA-Binding Protein
Homologous superfamily homologous superfamily10 — TATA-Binding Protein
Domain ID domain_id2iv9B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1150
Domain ID domain_id2iv9B02
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)