1ltx

Structure of Rab Escort Protein-1 in complex with Rab geranylgeranyl transferase and isoprenoid

Method: X-RAY DIFFRACTION Dmax: 144.8 Å Quality: GOOD

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

RAB GERANYLGERANYLTRANSFERASE ALPHA SUBUNIT

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–567 Not recorded RAB GERANYLGERANYLTRANSFERASE BETA SUBUNIT × 1 (Q08603) Rab Escort Protein 1 × 1 (P37727) AAAA × 1 ZN ZINC ION × 1 CL CHLORIDE ION × 1 FAR FARNESYL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;298 K;20% PEG 3350, 100mM KSCN, 100mM Namalonate, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.70 Å R-free 0.272

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 1–567; UniProt 1–567

RAB GERANYLGERANYLTRANSFERASE BETA SUBUNIT

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–331 Not recorded RAB GERANYLGERANYLTRANSFERASE ALPHA SUBUNIT × 1 (Q08602) Rab Escort Protein 1 × 1 (P37727) AAAA × 1 ZN ZINC ION × 1 CL CHLORIDE ION × 1 FAR FARNESYL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;298 K;20% PEG 3350, 100mM KSCN, 100mM Namalonate, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.70 Å R-free 0.272

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 PGTB_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–331; UniProt 1–331

Rab Escort Protein 1

Rattus norvegicus

UniProt P37727

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 R; UniProt 1–650 Mutation:A473T, G483A, Q231K RAB GERANYLGERANYLTRANSFERASE ALPHA SUBUNIT × 1 (Q08602) RAB GERANYLGERANYLTRANSFERASE BETA SUBUNIT × 1 (Q08603) AAAA × 1 ZN ZINC ION × 1 CL CHLORIDE ION × 1 FAR FARNESYL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;298 K;20% PEG 3350, 100mM KSCN, 100mM Namalonate, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.70 Å R-free 0.272

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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAE1_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain R; PDBConstruct 1–650; UniProt 1–650

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 1ltx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ltx
Deposition date deposition_date2002-05-21
Structure title titleStructure of Rab Escort Protein-1 in complex with Rab geranylgeranyl transferase and isoprenoid
Keywords keywordsRAB PRENYLATION, PRENYLTRANSFERASE, LUCINE-RICH REPEATS, POST-TRANSLATIONAL MODIFICATION, Transferase-Protein binding COMPLEX; Transferase/Protein binding
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.19
Radius of gyration Rg (electron density) rg_electron40.88
Forward intensity I(0) i0353185000.00
Molecular weight molecular_weight153210.0 kDa
Excluded volume excluded_volume191630 ų
Envelope volume envelope_volume248750 ų
Hydration-shell volume shell_volume52603 ų
Envelope diameter envelope_diameter152.4
Shell Rg shell_rg44.25
Envelope Rg envelope_rg40.49
Shape Rg shape_rg40.86
Total Rg total_rg41.15
Total atoms total_atoms10750
Residues n_residues1352
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 dmax144.8
Rg (real space) rg_real41.37
Rg uncertainty (real space) rg_real_error1.56
I(0) (real space) i0_real3.5320e+08
I(0) uncertainty (real space) i0_real_error6.7960e+06
Rg (reciprocal space) rg_reciprocal41.19
I(0) (reciprocal space) i0_reciprocal353100000.0000
Solution quality estimate total_estimate0.8579
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.9
Skewness Skewness skewness0.464
Kurtosis Kurtosis kurtosis-0.268
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha43500000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.798; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.948; Smooth: 0.808

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 13 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1ltxa1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.6 — Protein prenylyltransferase
Family Family familya.118.6.1 — Protein prenylyltransferase
Domain ID domain_idd1ltxa2
Class classb — All beta proteins
Fold Fold foldb.7 — C2 domain-like
Superfamily Superfamily superfamilyb.7.4 — Rab geranylgeranyltransferase alpha-subunit, insert domain
Family Family familyb.7.4.1 — Rab geranylgeranyltransferase alpha-subunit, insert domain
Domain ID domain_idd1ltxa3
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Superfamily Superfamily superfamilyc.10.2 — L domain-like
Family Family familyc.10.2.2 — Rab geranylgeranyltransferase alpha-subunit, C-terminal domain
Domain ID domain_idd1ltxb_
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
Domain ID domain_idd1ltxr1
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_idd1ltxr2
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

CATH v4.4 (7 domains)

Domain ID domain_id1ltxA01
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_id1ltxA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1130 — Rab geranylgeranyltransferase alpha-subunit, insert domain
Domain ID domain_id1ltxA03
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily10 — Ribonuclease Inhibitor
Domain ID domain_id1ltxB00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id1ltxR01
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_id1ltxR02
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_id1ltxR03
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 (2)

9. Files and Curves (10)