1lb1

Crystal Structure of the Dbl and Pleckstrin homology domains of Dbs in complex with RhoA

Method: X-RAY DIFFRACTION Dmax: 213.7 Å Quality: REASONABLE

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

Guanine nucleotide exchange factor DBS

Mus musculus

UniProt Q64096

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 623–967 Fragment:DBL homology domain (residues 623-818) and pleckstrin homology domain (residues 819-967) Transforming protein RhoA × 1 (P61586) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;292 K;PEG 3350, lithium citrate, Inositol 1,4,5-trisphosphate, pH 8.4, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.81 Å R-free 0.266
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 623–967 Fragment:DBL homology domain (residues 623-818) and pleckstrin homology domain (residues 819-967) Transforming protein RhoA × 1 (P61586) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;292 K;PEG 3350, lithium citrate, Inositol 1,4,5-trisphosphate, pH 8.4, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.81 Å R-free 0.266
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 623–967 Fragment:DBL homology domain (residues 623-818) and pleckstrin homology domain (residues 819-967) Transforming protein RhoA × 1 (P61586) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;292 K;PEG 3350, lithium citrate, Inositol 1,4,5-trisphosphate, pH 8.4, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.81 Å R-free 0.266
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 623–967 Fragment:DBL homology domain (residues 623-818) and pleckstrin homology domain (residues 819-967) Transforming protein RhoA × 1 (P61586) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;292 K;PEG 3350, lithium citrate, Inositol 1,4,5-trisphosphate, pH 8.4, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.81 Å R-free 0.266

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.

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCF2L_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–346; UniProt 623–967 Author chain C; PDBConstruct 2–346; UniProt 623–967 Author chain E; PDBConstruct 2–346; UniProt 623–967 Author chain G; PDBConstruct 2–346; UniProt 623–967

Transforming protein RhoA

Homo sapiens

UniProt P61586

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 1–190 Fragment:residues 1-190 Mutation:C190S Guanine nucleotide exchange factor DBS × 1 (Q64096) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;292 K;PEG 3350, lithium citrate, Inositol 1,4,5-trisphosphate, pH 8.4, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.81 Å R-free 0.266
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–190 Fragment:residues 1-190 Mutation:C190S Guanine nucleotide exchange factor DBS × 1 (Q64096) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;292 K;PEG 3350, lithium citrate, Inositol 1,4,5-trisphosphate, pH 8.4, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.81 Å R-free 0.266
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 1–190 Fragment:residues 1-190 Mutation:C190S Guanine nucleotide exchange factor DBS × 1 (Q64096) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;292 K;PEG 3350, lithium citrate, Inositol 1,4,5-trisphosphate, pH 8.4, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.81 Å R-free 0.266
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 1–190 Fragment:residues 1-190 Mutation:C190S Guanine nucleotide exchange factor DBS × 1 (Q64096) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;292 K;PEG 3350, lithium citrate, Inositol 1,4,5-trisphosphate, pH 8.4, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.81 Å R-free 0.266

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.

129 other PDB entries and 162 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RHOA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–192; UniProt 1–190 Author chain D; PDBConstruct 3–192; UniProt 1–190 Author chain F; PDBConstruct 3–192; UniProt 1–190 Author chain H; PDBConstruct 3–192; UniProt 1–190

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 1lb1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1lb1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1lb1
Deposition date deposition_date2002-04-01
Structure title titleCrystal Structure of the Dbl and Pleckstrin homology domains of Dbs in complex with RhoA
Keywords keywordsGUANINE NUCLEOTIDE EXCHANGE FACTOR, SMALL G-PROTEIN, RHOA, DBS, DH domain, PH domain, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier76.24
Radius of gyration Rg (electron density) rg_electron76.52
Forward intensity I(0) i0744487000.00
Molecular weight molecular_weight231490.0 kDa
Excluded volume excluded_volume290130 ų
Envelope volume envelope_volume546910 ų
Hydration-shell volume shell_volume63498 ų
Envelope diameter envelope_diameter234.8
Shell Rg shell_rg71.26
Envelope Rg envelope_rg71.28
Shape Rg shape_rg76.50
Total Rg total_rg76.50
Total atoms total_atoms16236
Residues n_residues2008
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 dmax213.7
Rg (real space) rg_real76.53
Rg uncertainty (real space) rg_real_error1.60
I(0) (real space) i0_real7.4440e+08
I(0) uncertainty (real space) i0_real_error1.3270e+07
Rg (reciprocal space) rg_reciprocal74.59
I(0) (reciprocal space) i0_reciprocal741200000.0000
Solution quality estimate total_estimate0.6931
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary96.2
Skewness Skewness skewness0.149
Kurtosis Kurtosis kurtosis-1.008
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.0005
Highest regularization parameter α highest_alpha12230000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.501; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.502; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

Domain ID domain_idd1lb1a1
Class classa — All alpha proteins
Fold Fold folda.87 — DBL homology domain (DH-domain)
Superfamily Superfamily superfamilya.87.1 — DBL homology domain (DH-domain)
Family Family familya.87.1.1 — DBL homology domain (DH-domain)
Domain ID domain_idd1lb1a2
Class classb — All beta proteins
Fold Fold foldb.55 — PH domain-like barrel
Superfamily Superfamily superfamilyb.55.1 — PH domain-like
Family Family familyb.55.1.1 — Pleckstrin-homology domain (PH domain)
Domain ID domain_idd1lb1b_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd1lb1c1
Class classa — All alpha proteins
Fold Fold folda.87 — DBL homology domain (DH-domain)
Superfamily Superfamily superfamilya.87.1 — DBL homology domain (DH-domain)
Family Family familya.87.1.1 — DBL homology domain (DH-domain)
Domain ID domain_idd1lb1c2
Class classb — All beta proteins
Fold Fold foldb.55 — PH domain-like barrel
Superfamily Superfamily superfamilyb.55.1 — PH domain-like
Family Family familyb.55.1.1 — Pleckstrin-homology domain (PH domain)
Domain ID domain_idd1lb1d_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd1lb1e1
Class classa — All alpha proteins
Fold Fold folda.87 — DBL homology domain (DH-domain)
Superfamily Superfamily superfamilya.87.1 — DBL homology domain (DH-domain)
Family Family familya.87.1.1 — DBL homology domain (DH-domain)
Domain ID domain_idd1lb1e2
Class classb — All beta proteins
Fold Fold foldb.55 — PH domain-like barrel
Superfamily Superfamily superfamilyb.55.1 — PH domain-like
Family Family familyb.55.1.1 — Pleckstrin-homology domain (PH domain)
Domain ID domain_idd1lb1f_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd1lb1g1
Class classa — All alpha proteins
Fold Fold folda.87 — DBL homology domain (DH-domain)
Superfamily Superfamily superfamilya.87.1 — DBL homology domain (DH-domain)
Family Family familya.87.1.1 — DBL homology domain (DH-domain)
Domain ID domain_idd1lb1g2
Class classb — All beta proteins
Fold Fold foldb.55 — PH domain-like barrel
Superfamily Superfamily superfamilyb.55.1 — PH domain-like
Family Family familyb.55.1.1 — Pleckstrin-homology domain (PH domain)
Domain ID domain_idd1lb1h_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins

CATH v4.4 (12 domains)

Domain ID domain_id1lb1A01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology900 — Dbl Homology Domain; Chain A
Homologous superfamily homologous superfamily10 — Dbl homology (DH) domain
Domain ID domain_id1lb1A02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Domain ID domain_id1lb1B00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id1lb1C01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology900 — Dbl Homology Domain; Chain A
Homologous superfamily homologous superfamily10 — Dbl homology (DH) domain
Domain ID domain_id1lb1C02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Domain ID domain_id1lb1D00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id1lb1E01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology900 — Dbl Homology Domain; Chain A
Homologous superfamily homologous superfamily10 — Dbl homology (DH) domain
Domain ID domain_id1lb1E02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Domain ID domain_id1lb1F00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id1lb1G01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology900 — Dbl Homology Domain; Chain A
Homologous superfamily homologous superfamily10 — Dbl homology (DH) domain
Domain ID domain_id1lb1G02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Domain ID domain_id1lb1H00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)