3dst

Crystal structure of RabGGTase(DELTA LRR; DELTA IG)in complex with geranylgeranyl pyrophosphate

Method: X-RAY DIFFRACTION Dmax: 87.9 Å Quality: GOOD

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

Geranylgeranyl transferase type-2 subunit alpha

Rattus norvegicus

UniProt Q08602

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 1–237 Chain A; UniProt 353–441 Fragment:PFTA domains, UNP residues 1-237 and 353-441 Geranylgeranyl transferase type-2 subunit beta × 1 (Q08603) GRG GERANYLGERANYL DIPHOSPHATE × 1 ZN ZINC ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;284 K;14% (w/v) PEG 3350, 0.2M Ca(OAc)2, 0.1M HEPES, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 284K Resolution 1.90 Å R-free 0.220

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.

20 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PGTA_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–238; UniProt 1–237 Author chain A; PDBConstruct 243–331; UniProt 353–441

Geranylgeranyl transferase type-2 subunit beta

Rattus norvegicus

UniProt Q08603

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 1–331 Not recorded Geranylgeranyl transferase type-2 subunit alpha × 1 (Q08602) GRG GERANYLGERANYL DIPHOSPHATE × 1 ZN ZINC ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;284 K;14% (w/v) PEG 3350, 0.2M Ca(OAc)2, 0.1M HEPES, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 284K Resolution 1.90 Å R-free 0.220

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.

20 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PGTB2_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–331; UniProt 1–331

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 3dst

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3dst
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3dst
Deposition date deposition_date2008-07-14
Structure title titleCrystal structure of RabGGTase(DELTA LRR; DELTA IG)in complex with geranylgeranyl pyrophosphate
Keywords keywordsprotein prenylation, Metal-binding, Prenyltransferase, Transferase, Zinc, Phosphoprotein; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.60
Radius of gyration Rg (electron density) rg_electron25.69
Forward intensity I(0) i082440600.00
Molecular weight molecular_weight71781.0 kDa
Excluded volume excluded_volume89970 ų
Envelope volume envelope_volume108140 ų
Hydration-shell volume shell_volume34256 ų
Envelope diameter envelope_diameter91.5
Shell Rg shell_rg33.79
Envelope Rg envelope_rg26.00
Shape Rg shape_rg25.68
Total Rg total_rg26.57
Total atoms total_atoms5046
Residues n_residues636
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 dmax87.9
Rg (real space) rg_real26.51
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real8.2440e+07
I(0) uncertainty (real space) i0_real_error1.0340e+06
Rg (reciprocal space) rg_reciprocal26.54
I(0) (reciprocal space) i0_reciprocal82440000.0000
Solution quality estimate total_estimate0.8854
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.2
Skewness Skewness skewness0.286
Kurtosis Kurtosis kurtosis-0.309
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20370000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.837; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3dstb_
Class classa — All alpha proteins
Fold Fold folda.102 — alpha/alpha toroid
Superfamily Superfamily superfamilya.102.4 — Terpenoid cyclases/Protein prenyltransferases
Family Family familya.102.4.3 — Protein prenyltransferases

CATH v4.4 (2 domains)

Domain ID domain_id3dstA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily120 — Protein prenylyltransferase
Domain ID domain_id3dstB00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)