SAXSdb — 1oeb

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

GRB2-RELATED ADAPTOR PROTEIN 2

MUS MUSCULUS

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 265–322	Fragment：SH3C DOMAIN, RESIDUES 265-322	LYMPHOCYTE CYTOSOLIC PROTEIN 2 × 1 （Q60787） CD CADMIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；PROTEIN WAS CRYSTALLISED FROM: 20% PEG4000, 5 MM CDCL2,50 MM NA CACODYLATE PH 6.5	Resolution 1.76 Å R-free 0.235
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 265–322	Fragment：SH3C DOMAIN, RESIDUES 265-322	LYMPHOCYTE CYTOSOLIC PROTEIN 2 × 1 （Q60787）	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；PROTEIN WAS CRYSTALLISED FROM: 20% PEG4000, 5 MM CDCL2,50 MM NA CACODYLATE PH 6.5	Resolution 1.76 Å R-free 0.235

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 1OEB	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1H3H Structural Basis for Specific Recognition of an RxxK-containing SLP-76 peptide by the Gads C-terminal SH3 domain Deposited 2002-09-03	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 263–322（60 aa） Fragment：C-TERMINAL SH3 DOMAIN, RESIDUES 263-322	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；285 K；Ionic strength (raw mmCIF value) 100MM NACL, 50MM SODIUM PHOSPHATE；Pressure 1	Resolution not provided
1R1P Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads Deposited 2003-09-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 50–147（98 aa） Fragment：Gads-SH2 domain	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 298K	Resolution 1.80 Å R-free 0.241
1R1P Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads Deposited 2003-09-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 50–147（98 aa） Fragment：Gads-SH2 domain	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 298K	Resolution 1.80 Å R-free 0.241
1R1P Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads Deposited 2003-09-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 50–147（98 aa） Fragment：Gads-SH2 domain	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 298K	Resolution 1.80 Å R-free 0.241
1R1P Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads Deposited 2003-09-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 50–147（98 aa） Fragment：Gads-SH2 domain	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 298K	Resolution 1.80 Å R-free 0.241
1R1Q Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads Deposited 2003-09-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 50–147（98 aa） Fragment：Gads-SH2 domain	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.7；298 K；0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.7, VAPOR DIFFUSION, temperature 298K	Resolution 1.80 Å R-free 0.225
1R1Q Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads Deposited 2003-09-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 50–147（98 aa） Fragment：Gads-SH2 domain	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.7；298 K；0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.7, VAPOR DIFFUSION, temperature 298K	Resolution 1.80 Å R-free 0.225
1R1Q Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads Deposited 2003-09-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 50–147（98 aa） Fragment：Gads-SH2 domain Chain B 50–147（98 aa） Fragment：Gads-SH2 domain	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.7；298 K；0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.7, VAPOR DIFFUSION, temperature 298K	Resolution 1.80 Å R-free 0.225
1R1S Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads Deposited 2003-09-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 50–147（98 aa） Fragment：Gads-SH2 domain	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 298K	Resolution 1.90 Å R-free 0.259
1R1S Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads Deposited 2003-09-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 50–147（98 aa） Fragment：Gads-SH2 domain	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 298K	Resolution 1.90 Å R-free 0.259
1R1S Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads Deposited 2003-09-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 50–147（98 aa） Fragment：Gads-SH2 domain	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 298K	Resolution 1.90 Å R-free 0.259
1R1S Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads Deposited 2003-09-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 50–147（98 aa） Fragment：Gads-SH2 domain	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 298K	Resolution 1.90 Å R-free 0.259
1R1S Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads Deposited 2003-09-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 50–147（98 aa） Fragment：Gads-SH2 domain Chain E 50–147（98 aa） Fragment：Gads-SH2 domain	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 298K	Resolution 1.90 Å R-free 0.259
1R1S Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads Deposited 2003-09-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 50–147（98 aa） Fragment：Gads-SH2 domain Chain G 50–147（98 aa） Fragment：Gads-SH2 domain	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 298K	Resolution 1.90 Å R-free 0.259
1UTI Mona/Gads SH3C in complex with HPK derived peptide Deposited 2003-12-09	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 265–322（58 aa） Fragment：SH3C DOMAIN, RESIDUES 265-322	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；2M AMMONIUM SULFATE, 0.05M HEPES PH7.5, pH 7.50	Resolution 1.50 Å R-free 0.221
2D0N Crystal structure of the C-terminal SH3 domain of the adaptor protein GADS in complex with SLP-76 motif peptide reveals a unique SH3-SH3 interaction Deposited 2005-08-04	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 267–322（56 aa） Fragment：C-terminal SH3 domain Chain C 267–322（56 aa） Fragment：C-terminal SH3 domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；1.26M ammonium sulfate, 0.1M cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.57 Å R-free 0.284
2W10 Mona SH3C in complex Deposited 2008-10-13	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 265–322（58 aa） Fragment：SH3 2, RESIDUES 265-322	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；0.1 M PHOSPHATE CITRATE, 2 M AMMONIUM SULPHATE, pH 7.5	Resolution 1.90 Å R-free 0.231
2W10 Mona SH3C in complex Deposited 2008-10-13	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 265–322（58 aa） Fragment：SH3 2, RESIDUES 265-322	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；0.1 M PHOSPHATE CITRATE, 2 M AMMONIUM SULPHATE, pH 7.5	Resolution 1.90 Å R-free 0.231

7 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GRP2_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–62； UniProt 265–322 Author chain B； PDBConstruct 5–62； UniProt 265–322

LYMPHOCYTE CYTOSOLIC PROTEIN 2

OrganismNot specified

UniProt Q60787

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 231–243	Fragment：PROTEIN INTERACTION PEPTIDE, RESIDUES 231-243	GRB2-RELATED ADAPTOR PROTEIN 2 × 1 （O89100） CD CADMIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；PROTEIN WAS CRYSTALLISED FROM: 20% PEG4000, 5 MM CDCL2,50 MM NA CACODYLATE PH 6.5	Resolution 1.76 Å R-free 0.235
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 231–243	Fragment：PROTEIN INTERACTION PEPTIDE, RESIDUES 231-243	GRB2-RELATED ADAPTOR PROTEIN 2 × 1 （O89100）	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；PROTEIN WAS CRYSTALLISED FROM: 20% PEG4000, 5 MM CDCL2,50 MM NA CACODYLATE PH 6.5	Resolution 1.76 Å R-free 0.235

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 1OEB	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2ETZ The NMR minimized average structure of the Itk SH2 domain bound to a phosphopeptide Deposited 2005-10-27	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 143–148（6 aa） Fragment：phosphopeptide fragment sequence database residues 143-148	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 125mM；Pressure ambient NMR sample composition 1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 \| 90% H2O/10% D2O NMR sample composition U-15N labeled, 1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 \| 90% H2O/10% D2O NMR sample composition U-15N, 13-C labeled, 1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 \| 90%H20, 10%D2O NMR sample composition 5mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 \| 90%H20, 10%D2O NMR sample composition 1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 \| 100% D2O	Resolution not provided
2EU0 The NMR ensemble structure of the Itk SH2 domain bound to a phosphopeptide Deposited 2005-10-27	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 143–148（6 aa） Fragment：phosphopeptide fragment, sequence database residues 143-148	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 125mM；Pressure ambient NMR sample composition 1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 \| 90% H2O/10% D2O NMR sample composition U-15N labeled, 1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 \| 90% H2O/10% D2O NMR sample composition U-15N, 13-C labeled, 1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 \| 90% H2O/10% D2O NMR sample composition 5mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 \| 90%H20, 10%D2O NMR sample composition 1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 \| 100% D2O	Resolution not provided

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

View Construct and Data Evidence

UniProt name	LCP2_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–13； UniProt 231–243 Author chain D； PDBConstruct 1–13； UniProt 231–243

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1oeb
Deposition date deposition_date	2003-03-24
Structure title title	Mona/Gads SH3C domain
Keywords keywords	PROTEIN BINDING, SH3 DOMAIN-COMPLEX, SH3, SLP-76, DIMER, MONA, GADS, SIGNAL TRANDUCTION; PROTEIN BINDING
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	17.34 Å
Radius of gyration Rg (electron density) rg_electron	16.63 Å
Forward intensity I(0) i0	4663430.00
Molecular weight molecular_weight	15597.0 kDa
Excluded volume excluded_volume	19473 Å³
Envelope volume envelope_volume	22749 Å³
Hydration-shell volume shell_volume	12350 Å³
Envelope diameter envelope_diameter	59.3 Å
Shell Rg shell_rg	21.30 Å
Envelope Rg envelope_rg	16.83 Å
Shape Rg shape_rg	16.64 Å
Total Rg total_rg	17.44 Å
Total atoms total_atoms	1099
Residues n_residues	138
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	58.4 Å
Rg (real space) rg_real	17.42 Å
Rg uncertainty (real space) rg_real_error	0.40 Å
I(0) (real space) i0_real	4.6630e+06
I(0) uncertainty (real space) i0_real_error	6.1690e+04
Rg (reciprocal space) rg_reciprocal	17.41 Å
I(0) (reciprocal space) i0_reciprocal	4663000.0000
Solution quality estimate total_estimate	0.7731
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	18.4 Å
Skewness Skewness skewness	0.486
Kurtosis Kurtosis kurtosis	-0.269
Angular range angular_range	— – 0.4600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1690000.0000
Real-space data points n_real_points	77
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.718; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.894; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	GRB2-RELATED ADAPTOR PROTEIN 2
Molecular weight formula_weight	7089.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	1337

PLGSVRWARALYDFEALEEDELGFRSGEVVEVLDSSNPSWWTGRLHNKLGLFPANYVAPMMR

来源 Source

来源生物 organism	MUS MUSCULUS
通用名 common_name	MOUSE
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	LYMPHOCYTE CYTOSOLIC PROTEIN 2
Molecular weight formula_weight	1380.6 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

PAPSIDRSTKPPL

Entity 3 Entity 3 non-polymer

Description description	CADMIUM ION
Molecular weight formula_weight	112.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	238

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1oeba_
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.2 — SH3-domain
Family Family family	b.34.2.1 — SH3-domain

Domain ID domain_id	d1oebb_
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.2 — SH3-domain
Family Family family	b.34.2.1 — SH3-domain

CATH v4.4 (2 domains)

Domain ID domain_id	1oebA00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	40 — SH3 Domains

Domain ID domain_id	1oebB00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	40 — SH3 Domains

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8. Citations (1)

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Unit-cell length a length_a	28.691 Å
Unit-cell length b length_b	72.072 Å
Unit-cell length c length_c	34.168 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	97.70 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.760 Å
Low-resolution limit resolution_low	19.690 Å
R factor r_factor	0.1740
R_work r_work	0.1710
R_free r_free	0.2350

fit	/app/data/saxs_computation/oe/1oeb/1oeb.fit
pddf	/app/data/pr_computation/oe/1oeb/1oeb.pr.out
profile	/app/data/saxs_computation/oe/1oeb/1oeb.dat

Mona/Gads SH3C domain

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

GRB2-RELATED ADAPTOR PROTEIN 2

State in the Current Structure

Other States of the Same Protein in the Database

LYMPHOCYTE CYTOSOLIC PROTEIN 2

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)