1lv0

Crystal structure of the Rab effector guanine nucleotide dissociation inhibitor (GDI) in complex with a geranylgeranyl (GG) peptide

Method: X-RAY DIFFRACTION Dmax: 78.6 Å Quality: GOOD

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

RAB GDP disossociation inhibitor alpha

Bos taurus

UniProt P21856

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–447 Not recorded SO4 SULFATE ION × 3 GER GERAN-8-YL GERAN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.2;296 K;Ammonium Sulfate, pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 296K Resolution 2.00 Å R-free 0.249

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GDIA_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–449; UniProt 1–447

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 1lv0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1lv0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1lv0
Deposition date deposition_date2002-05-23
Structure title titleCrystal structure of the Rab effector guanine nucleotide dissociation inhibitor (GDI) in complex with a geranylgeranyl (GG) peptide
Keywords keywordsProtein-ligand complex, 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_guinier23.67
Radius of gyration Rg (electron density) rg_electron22.59
Forward intensity I(0) i040537800.00
Molecular weight molecular_weight49408.0 kDa
Excluded volume excluded_volume61922 ų
Envelope volume envelope_volume72419 ų
Hydration-shell volume shell_volume26548 ų
Envelope diameter envelope_diameter81.5
Shell Rg shell_rg29.88
Envelope Rg envelope_rg22.82
Shape Rg shape_rg22.58
Total Rg total_rg23.49
Total atoms total_atoms3466
Residues n_residues432
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 dmax78.6
Rg (real space) rg_real23.59
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real4.0540e+07
I(0) uncertainty (real space) i0_real_error4.9270e+05
Rg (reciprocal space) rg_reciprocal23.61
I(0) (reciprocal space) i0_reciprocal40540000.0000
Solution quality estimate total_estimate0.8110
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.0
Skewness Skewness skewness0.257
Kurtosis Kurtosis kurtosis-0.394
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10540000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1lv0a1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamilyc.3.1 — FAD/NAD(P)-binding domain
Family Family familyc.3.1.3 — GDI-like N domain
Domain ID domain_idd1lv0a2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.16 — FAD-linked reductases, C-terminal domain
Superfamily Superfamily superfamilyd.16.1 — FAD-linked reductases, C-terminal domain
Family Family familyd.16.1.6 — GDI-like
Domain ID domain_idd1lv0a3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (3 domains)

Domain ID domain_id1lv0A01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1lv0A02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology519 — Guanine Nucleotide Dissociation Inhibitor; domain 2
Homologous superfamily homologous superfamily10 — Guanine Nucleotide Dissociation Inhibitor, domain 2
Domain ID domain_id1lv0A03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology405 — Guanine Nucleotide Dissociation Inhibitor; domain 1
Homologous superfamily homologous superfamily10 — Guanine Nucleotide Dissociation Inhibitor, domain 1

8. Citations (1)

9. Files and Curves (10)