1fyr

DIMER FORMATION THROUGH DOMAIN SWAPPING IN THE CRYSTAL STRUCTURE OF THE GRB2-SH2 AC-PYVNV COMPLEX

Method: X-RAY DIFFRACTION Dmax: 69.8 Å Quality: EXCELLENT

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

GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2

Homo sapiens

UniProt P29354

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 50–161 Chain B; UniProt 50–161 Fragment:SH2 DOMAIN HEPATOCYTE GROWTH FACTOR RECEPTOR PEPTIDE × 2 (P08581) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;298 K;11% PEG 3350, 0.5M NaCL, 0.1M MES/NaOH pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.40 Å R-free 0.270
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 50–161 Chain D; UniProt 50–161 Fragment:SH2 DOMAIN HEPATOCYTE GROWTH FACTOR RECEPTOR PEPTIDE × 2 (P08581) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;298 K;11% PEG 3350, 0.5M NaCL, 0.1M MES/NaOH pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.40 Å R-free 0.270
3 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 50–161 Chain B; UniProt 50–161 Chain C; UniProt 50–161 Chain D; UniProt 50–161 Fragment:SH2 DOMAIN HEPATOCYTE GROWTH FACTOR RECEPTOR PEPTIDE × 4 (P08581) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;298 K;11% PEG 3350, 0.5M NaCL, 0.1M MES/NaOH pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.40 Å R-free 0.270
4 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 50–161 Chain B; UniProt 50–161 Chain C; UniProt 50–161 Chain D; UniProt 50–161 Fragment:SH2 DOMAIN HEPATOCYTE GROWTH FACTOR RECEPTOR PEPTIDE × 4 (P08581) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;298 K;11% PEG 3350, 0.5M NaCL, 0.1M MES/NaOH pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.40 Å R-free 0.270
5 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 50–161 Chain B; UniProt 50–161 Chain C; UniProt 50–161 Fragment:SH2 DOMAIN HEPATOCYTE GROWTH FACTOR RECEPTOR PEPTIDE × 3 (P08581) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;298 K;11% PEG 3350, 0.5M NaCL, 0.1M MES/NaOH pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.40 Å R-free 0.270
6 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 50–161 Chain C; UniProt 50–161 Chain D; UniProt 50–161 Fragment:SH2 DOMAIN HEPATOCYTE GROWTH FACTOR RECEPTOR PEPTIDE × 3 (P08581) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;298 K;11% PEG 3350, 0.5M NaCL, 0.1M MES/NaOH pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.40 Å R-free 0.270

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.

3 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRB2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–114; UniProt 50–161 Author chain B; PDBConstruct 3–114; UniProt 50–161 Author chain C; PDBConstruct 3–114; UniProt 50–161 Author chain D; PDBConstruct 3–114; UniProt 50–161

HEPATOCYTE GROWTH FACTOR RECEPTOR PEPTIDE

OrganismNot specified

UniProt P08581

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain I; UniProt 1356–1359 Chain J; UniProt 1356–1359 Fragment:RESIDUES 1356-1359 (RESIDUES 0-3 IN COORDINATES) Non-standard monomer:Yes (specific site not provided by mmCIF) GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2 × 2 (P29354) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;298 K;11% PEG 3350, 0.5M NaCL, 0.1M MES/NaOH pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.40 Å R-free 0.270
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain K; UniProt 1356–1359 Chain L; UniProt 1356–1359 Fragment:RESIDUES 1356-1359 (RESIDUES 0-3 IN COORDINATES) Non-standard monomer:Yes (specific site not provided by mmCIF) GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2 × 2 (P29354) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;298 K;11% PEG 3350, 0.5M NaCL, 0.1M MES/NaOH pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.40 Å R-free 0.270
3 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain I; UniProt 1356–1359 Chain J; UniProt 1356–1359 Chain K; UniProt 1356–1359 Chain L; UniProt 1356–1359 Fragment:RESIDUES 1356-1359 (RESIDUES 0-3 IN COORDINATES) Non-standard monomer:Yes (specific site not provided by mmCIF) GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2 × 4 (P29354) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;298 K;11% PEG 3350, 0.5M NaCL, 0.1M MES/NaOH pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.40 Å R-free 0.270
4 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain I; UniProt 1356–1359 Chain J; UniProt 1356–1359 Chain K; UniProt 1356–1359 Chain L; UniProt 1356–1359 Fragment:RESIDUES 1356-1359 (RESIDUES 0-3 IN COORDINATES) Non-standard monomer:Yes (specific site not provided by mmCIF) GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2 × 4 (P29354) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;298 K;11% PEG 3350, 0.5M NaCL, 0.1M MES/NaOH pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.40 Å R-free 0.270
5 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain I; UniProt 1356–1359 Chain J; UniProt 1356–1359 Chain K; UniProt 1356–1359 Fragment:RESIDUES 1356-1359 (RESIDUES 0-3 IN COORDINATES) Non-standard monomer:Yes (specific site not provided by mmCIF) GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2 × 3 (P29354) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;298 K;11% PEG 3350, 0.5M NaCL, 0.1M MES/NaOH pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.40 Å R-free 0.270
6 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain J; UniProt 1356–1359 Chain K; UniProt 1356–1359 Chain L; UniProt 1356–1359 Fragment:RESIDUES 1356-1359 (RESIDUES 0-3 IN COORDINATES) Non-standard monomer:Yes (specific site not provided by mmCIF) GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2 × 3 (P29354) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;298 K;11% PEG 3350, 0.5M NaCL, 0.1M MES/NaOH pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.40 Å R-free 0.270

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.

128 other PDB entries and 161 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MET_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 2–5; UniProt 1356–1359 Author chain J; PDBConstruct 2–5; UniProt 1356–1359 Author chain K; PDBConstruct 2–5; UniProt 1356–1359 Author chain L; PDBConstruct 2–5; UniProt 1356–1359

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 1fyr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1fyr
Deposition date deposition_date2000-10-03
Structure title titleDIMER FORMATION THROUGH DOMAIN SWAPPING IN THE CRYSTAL STRUCTURE OF THE GRB2-SH2 AC-PYVNV COMPLEX
Keywords keywordsGrb2, SH2 domain, phosphopeptide, Met, domain swapping, dimerization, HORMONE-GROWTH FACTOR COMPLEX; HORMONE/GROWTH FACTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.47
Radius of gyration Rg (electron density) rg_electron22.42
Forward intensity I(0) i037812100.00
Molecular weight molecular_weight47412.0 kDa
Excluded volume excluded_volume59405 ų
Envelope volume envelope_volume72053 ų
Hydration-shell volume shell_volume26637 ų
Envelope diameter envelope_diameter72.0
Shell Rg shell_rg29.59
Envelope Rg envelope_rg22.35
Shape Rg shape_rg22.34
Total Rg total_rg23.54
Total atoms total_atoms3356
Residues n_residues398
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 dmax69.8
Rg (real space) rg_real23.29
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real3.7810e+07
I(0) uncertainty (real space) i0_real_error5.0090e+05
Rg (reciprocal space) rg_reciprocal23.34
I(0) (reciprocal space) i0_reciprocal37810000.0000
Solution quality estimate total_estimate0.9111
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.2
Skewness Skewness skewness0.033
Kurtosis Kurtosis kurtosis-0.606
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7846000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.955; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1fyra_
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_idd1fyrb_
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_idd1fyrc_
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_idd1fyrd_
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

CATH v4.4 (4 domains)

Domain ID domain_id1fyrA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain
Domain ID domain_id1fyrB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain
Domain ID domain_id1fyrC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain
Domain ID domain_id1fyrD00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain

8. Citations (1)

9. Files and Curves (10)