4jvs

Crystal structure of LepB GAP domain from Legionella drancourtii in complex with Rab1-GDP and AlF3

Method: X-RAY DIFFRACTION Dmax: 78.4 Å Quality: GOOD

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

Putative uncharacterized protein

Legionella drancourtii

UniProt G9EPL4

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 316–620 Fragment:GAP domain, UNP residues 316-620 Ras-related protein Rab-1A × 1 (P62820) ACY ACETIC ACID × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 8.5;298 K;0.2M ammonium acetate, 0.1M Tris, 25%(w/v) polyethylene glycol 3350, pH 8.5, EVAPORATION, temperature 298.0K Resolution 2.78 Å R-free 0.265

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name G9EPL4_9GAMM
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–310; UniProt 316–620

Ras-related protein Rab-1A

Homo sapiens

UniProt P62820

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 1–177 Fragment:UNP residues 1-177 Putative uncharacterized protein × 1 (G9EPL4) ACY ACETIC ACID × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 8.5;298 K;0.2M ammonium acetate, 0.1M Tris, 25%(w/v) polyethylene glycol 3350, pH 8.5, EVAPORATION, temperature 298.0K Resolution 2.78 Å R-free 0.265

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.

14 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAB1A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–181; UniProt 1–177

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 4jvs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4jvs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4jvs
Deposition date deposition_date2013-03-26
Structure title titleCrystal structure of LepB GAP domain from Legionella drancourtii in complex with Rab1-GDP and AlF3
Keywords keywordsNew GAP fold, Bind and hydrolyze guanosine triphosphate, Rab1 Binding, HYDROLASE ACTIVATOR-PROTEIN TRANSPORT complex; HYDROLASE ACTIVATOR/PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.35
Radius of gyration Rg (electron density) rg_electron23.35
Forward intensity I(0) i046467200.00
Molecular weight molecular_weight51949.0 kDa
Excluded volume excluded_volume64663 ų
Envelope volume envelope_volume77629 ų
Hydration-shell volume shell_volume27457 ų
Envelope diameter envelope_diameter79.6
Shell Rg shell_rg30.71
Envelope Rg envelope_rg23.62
Shape Rg shape_rg23.34
Total Rg total_rg24.25
Total atoms total_atoms3651
Residues n_residues449
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 dmax78.4
Rg (real space) rg_real24.26
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real4.6470e+07
I(0) uncertainty (real space) i0_real_error5.7380e+05
Rg (reciprocal space) rg_reciprocal24.29
I(0) (reciprocal space) i0_reciprocal46470000.0000
Solution quality estimate total_estimate0.8982
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.254
Kurtosis Kurtosis kurtosis-0.405
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha14610000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4jvsb_
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 (3 domains)

Domain ID domain_id4jvsA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily1700
Domain ID domain_id4jvsA02
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily830
Domain ID domain_id4jvsB00
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)