SAXSdb — 1h3h

▼

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 263–322	Fragment：C-TERMINAL SH3 DOMAIN, RESIDUES 263-322	LYMPHOCYTE CYTOSOLIC PROTEIN 2 × 1 （Q13094）	SOLUTION NMR NMR measurement conditions：pH 6；285 K；Ionic strength (raw mmCIF value) 100MM NACL, 50MM SODIUM PHOSPHATE；Pressure 1	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 1H3H	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1OEB Mona/Gads SH3C domain Deposited 2003-03-24	Different construct Different ligand/ion Different experimental method 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	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
1OEB Mona/Gads SH3C domain Deposited 2003-03-24	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 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 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
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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 construct Different experimental method 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 method 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 method 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 method 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 19 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 1–60； UniProt 263–322

LYMPHOCYTE CYTOSOLIC PROTEIN 2

HOMO SAPIENS

UniProt Q13094

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 B； UniProt 226–235	Fragment：RESIDUES 226-235	GRB2-RELATED ADAPTOR PROTEIN 2 × 1 （O89100）	SOLUTION NMR NMR measurement conditions：pH 6；285 K；Ionic strength (raw mmCIF value) 100MM NACL, 50MM SODIUM PHOSPHATE；Pressure 1	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 1H3H	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1YWO Phospholipase Cgamma1 SH3 in complex with a SLP-76 motif Deposited 2005-02-18	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain P 185–194（10 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；malonate , pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.81 Å R-free 0.221
2EAP Solution structure of the N-terminal SAM-domain of human lymphocyte cytosolic protein 2 Deposited 2007-01-31	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–83（83 aa） Fragment：N-terminal SAM domain, residues 8-90	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；296 K；Ionic strength (raw mmCIF value) 120mM；Pressure AMBIENT NMR sample composition 1.16mM SAM DOMAIN; 20mM d-TRIS-HCL; 100mM NaCl; 1mM d-DTT; 0.02 % NaN3; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2ROR Solution structure of the VAV1 SH2 domain complexed with a tyrosine-phosphorylated peptide from SLP76 Deposited 2008-04-08	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 122–136（15 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；296 K；Ionic strength (raw mmCIF value) 120；Pressure ambient NMR sample composition 1.08mM [U-13C; U-15N] Proto-oncogene vav; 1.08mM tyrosine-phosphorylated peptide; 20mM [U-2H] TRIS; 100mM sodium chloride; 0.02% sodium azide; 1mM [U-2H] DTT; 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	LCP2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–10； UniProt 226–235

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1h3h
Deposition date deposition_date	2002-09-03
Structure title title	Structural Basis for Specific Recognition of an RxxK-containing SLP-76 peptide by the Gads C-terminal SH3 domain
Keywords keywords	PROTEIN-BINDING, COMPLEX (SH3-PEPTIDE), T-CELL SIGNALING, SH3 DOMAIN, SH2 DOMAIN, PROTEIN BINDING; PROTEIN BINDING
Experimental Method method	SOLUTION NMR

▼

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

Radius of gyration Rg (Guinier) rg_guinier	11.66 Å
Radius of gyration Rg (electron density) rg_electron	11.24 Å
Forward intensity I(0) i0	376595000.00
Molecular weight molecular_weight	161640.0 kDa
Excluded volume excluded_volume	201020 Å³
Envelope volume envelope_volume	15346 Å³
Hydration-shell volume shell_volume	10445 Å³
Envelope diameter envelope_diameter	41.1 Å
Shell Rg shell_rg	18.27 Å
Envelope Rg envelope_rg	12.95 Å
Shape Rg shape_rg	11.15 Å
Total Rg total_rg	11.68 Å
Total atoms total_atoms	22500
Residues n_residues	1420
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

▼

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

Maximum dimension Dmax dmax	36.7 Å
Rg (real space) rg_real	11.58 Å
Rg uncertainty (real space) rg_real_error	0.29 Å
I(0) (real space) i0_real	3.7660e+08
I(0) uncertainty (real space) i0_real_error	3.7960e+06
Rg (reciprocal space) rg_reciprocal	11.58 Å
I(0) (reciprocal space) i0_reciprocal	376600000.0000
Solution quality estimate total_estimate	0.8126
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	15.8 Å
Skewness Skewness skewness	0.103
Kurtosis Kurtosis kurtosis	-0.316
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	141200.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.859; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	GRB2-RELATED ADAPTOR PROTEIN 2
Molecular weight formula_weight	6948.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	22500

GRVRWARALYDFEALEEDELGFRSGEVVEVLDSSNPSWWTGRLHNKLGLFPANYVAPMMR

来源 Source

来源生物 organism	MUS MUSCULUS
通用名 common_name	HOUSE 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	1144.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

APSIDRSTKPA

来源 Source

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	ESCHERICHIA COLI

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1h3ha_
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 (1 domains)

Domain ID domain_id	1h3hA00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	40 — SH3 Domains

▶

8. Citations (2)

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

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

fit	/app/data/saxs_computation/h3/1h3h/1h3h.fit
pddf	/app/data/pr_computation/h3/1h3h/1h3h.pr.out
profile	/app/data/saxs_computation/h3/1h3h/1h3h.dat

Structural Basis for Specific Recognition of an RxxK-containing SLP-76 peptide by the Gads C-terminal SH3 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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)