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1qjt

SOLUTION STRUCTURE OF THE APO EH1 DOMAIN OF MOUSE EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15, EPS15

Method: SOLUTION NMR Dmax: 57.6 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE SUBSTRATE 15, EPS15

MUS MUSCULUS

UniProt P42567

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 7–105 Fragment：N-TERMINAL EH1 DOMAIN RESIDUES 1-120 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 5.2；298 K；Ionic strength (raw mmCIF value) 100 mM NaCl；Pressure 1 NMR sample composition：90% H2O/10% D2O Resolution not provided

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.

Other PDB Difference from Current Entry 1QJT Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1KYF AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPS15 DPF PEPTIDE Deposited 2002-02-04 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain P 627–632（6 aa） Fragment：RESIDUES 628-632
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.22 Å R-free 0.211
1KYU AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPS15 DPF PEPTIDE Deposited 2002-02-05 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain P 628–632（5 aa） Fragment：RESIDUES 628-632
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å R-free 0.223

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EP15_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–99； UniProt 7–105

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 1qjt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1qjt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1qjt
Deposition date deposition_date1999-07-02
Structure title titleSOLUTION STRUCTURE OF THE APO EH1 DOMAIN OF MOUSE EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15, EPS15
Keywords keywordsGROWTH FACTOR, EH DOMAIN, EPS15, EF-HAND, SOLUTION STRUCTURE, S100 PROTEIN; GROWTH FACTOR
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier18.29 Å
Radius of gyration Rg (electron density) rg_electron17.91 Å
Forward intensity I(0) i01292340000.00
Molecular weight molecular_weight319330.0 kDa
Excluded volume excluded_volume406230 ų
Envelope volume envelope_volume81853 ų
Hydration-shell volume shell_volume30199 ų
Envelope diameter envelope_diameter62.2 Å
Shell Rg shell_rg29.73 Å
Envelope Rg envelope_rg21.41 Å
Shape Rg shape_rg17.89 Å
Total Rg total_rg18.27 Å
Total atoms total_atoms45270
Residues n_residues2970
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax57.6 Å
Rg (real space) rg_real18.19 Å
Rg uncertainty (real space) rg_real_error0.23 Å
I(0) (real space) i0_real1.2920e+09
I(0) uncertainty (real space) i0_real_error1.4290e+07
Rg (reciprocal space) rg_reciprocal18.21 Å
I(0) (reciprocal space) i0_reciprocal1292000000.0000
Solution quality estimate total_estimate0.7380
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.0 Å
Skewness Skewness skewness0.198
Kurtosis Kurtosis kurtosis-0.475
Angular range angular_range— – 0.4350 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26040000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 0.330; Positv: 1.000; Valcen: 0.991; Smooth: 0.957
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1qjta_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.6 — Eps15 homology domain (EH domain)

CATH v4.4 (1 domains)

Domain ID domain_id1qjtA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
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8. Citations (2)

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9. Files and Curves (10)