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1mil

TRANSFORMING PROTEIN

Method: X-RAY DIFFRACTION Dmax: 44.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

SHC ADAPTOR PROTEIN

Homo sapiens

UniProt P29353

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 482–583 Fragment：PHOSPHOTYROSINE RECOGNITION DOMAIN SH2 No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.70 Å

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 1MIL Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1N3H Coupling of Folding and Binding in the PTB Domain of the Signaling Protein Shc Deposited 2002-10-28 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 111–317（207 aa） Fragment：PTB domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 200mM；Pressure 1
NMR sample composition 0.5mM Shc PTB Domain, 50mM Sodium phosphate, 20mM DTT-d10, pH 6.5 | 90% H2O/10% D2O
Resolution not provided
1OY2 Coupling of Folding and Binding in the PTB Domain of the Signaling Protein Shc Deposited 2003-04-03 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 111–317（207 aa） Fragment：PTB Domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 200mM；Pressure 1
NMR sample composition 0.5mM Shc PTB Domain, 50mM Sodium phosphate, 20mM DTT-d10 | 90% D2O, 10% D2O
Resolution not provided
1QG1 GROWTH FACTOR RECEPTOR BINDING PROTEIN SH2 DOMAIN COMPLEXED WITH AN SHC-DERIVED PEPTIDE Deposited 1999-04-19 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain I 423–435（13 aa） Fragment：423-435
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.3；301 K
Resolution not provided
1SHC SHC PTB DOMAIN COMPLEXED WITH A TRKA RECEPTOR PHOSPHOPEPTIDE, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1996-03-27 Different construct Different oligomeric state Different experimental method Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 126–317（192 aa） Fragment：PTB DOMAIN
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1TCE SOLUTION NMR STRUCTURE OF THE SHC SH2 DOMAIN COMPLEXED WITH A TYROSINE-PHOSPHORYLATED PEPTIDE FROM THE T-CELL RECEPTOR, MINIMIZED AVERAGE STRUCTURE Deposited 1996-03-27 Different construct Different oligomeric state Different experimental method Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 480–583（104 aa） Fragment：SH2 DOMAIN
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
4JMH Crystal structure of synthetic protein in complex with double pY peptide Deposited 2013-03-14 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 344–356（13 aa） Fragment：unp residues 344-356
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.66% ammonium sulfate, 2.32% PEG400, 0.1 M HEPES , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.41 Å R-free 0.276
4XWX Crystal structure of the PTB domain of SHC Deposited 2015-01-29 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–201（165 aa） Fragment：residues 37-201
Not recorded EDO 1,2-ETHANEDIOL × 6 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277.15 K；0.8 M sodium/potassium tartrate, 0.1 M Hepes pH 7.5
Resolution 1.87 Å R-free 0.191

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SHC1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 3–104； UniProt 482–583

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 1mil

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1mil
Deposition date deposition_date1995-09-20
Structure title titleTRANSFORMING PROTEIN
Keywords keywordsSH2 DOMAIN, PHOSPHORYLATION, COLLAGEN, GROWTH REGULATION, TRANSFORMING PROTEIN, ALTERNATIVE INITIATION; TRANSFORMING PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.43 Å
Radius of gyration Rg (electron density) rg_electron12.86 Å
Forward intensity I(0) i02778770.00
Molecular weight molecular_weight11377.0 kDa
Excluded volume excluded_volume14186 ų
Envelope volume envelope_volume16116 ų
Hydration-shell volume shell_volume10731 ų
Envelope diameter envelope_diameter41.7 Å
Shell Rg shell_rg18.49 Å
Envelope Rg envelope_rg13.18 Å
Shape Rg shape_rg12.83 Å
Total Rg total_rg14.22 Å
Total atoms total_atoms803
Residues n_residues104
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 dmax44.3 Å
Rg (real space) rg_real14.31 Å
Rg uncertainty (real space) rg_real_error0.23 Å
I(0) (real space) i0_real2.7790e+06
I(0) uncertainty (real space) i0_real_error2.8990e+04
Rg (reciprocal space) rg_reciprocal14.32 Å
I(0) (reciprocal space) i0_reciprocal2779000.0000
Solution quality estimate total_estimate0.8935
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.2 Å
Skewness Skewness skewness0.023
Kurtosis Kurtosis kurtosis-0.394
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha430900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.984
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1mila1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.93 — SH2-like
Superfamily Superfamily superfamilyd.93.1 — SH2 domain
Family Family familyd.93.1.1 — SH2 domain
Domain ID domain_idd1mila2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1milA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain
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8. Citations (4)

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9. Files and Curves (10)