1dce

CRYSTAL STRUCTURE OF RAB GERANYLGERANYLTRANSFERASE FROM RAT BRAIN

Method: X-RAY DIFFRACTION Dmax: 142.6 Å Quality: GOOD

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

PROTEIN (RAB GERANYLGERANYLTRANSFERASE ALPHA SUBUNIT)

OrganismNot specified

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 1–567 Non-standard monomer:Yes (specific site not provided by mmCIF) PROTEIN (RAB GERANYLGERANYLTRANSFERASE BETA SUBUNIT) × 1 (Q08603) ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å R-free 0.263
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–567 Non-standard monomer:Yes (specific site not provided by mmCIF) PROTEIN (RAB GERANYLGERANYLTRANSFERASE BETA SUBUNIT) × 1 (Q08603) ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å R-free 0.263

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 20 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 Author chain C; PDBConstruct 1–567; UniProt 1–567

PROTEIN (RAB GERANYLGERANYLTRANSFERASE BETA SUBUNIT)

OrganismNot specified

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 PROTEIN (RAB GERANYLGERANYLTRANSFERASE ALPHA SUBUNIT) × 1 (Q08602) ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å R-free 0.263
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–331 Not recorded PROTEIN (RAB GERANYLGERANYLTRANSFERASE ALPHA SUBUNIT) × 1 (Q08602) ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å R-free 0.263

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 20 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 Author chain D; 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 1dce

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1dce
Deposition date deposition_date1999-11-04
Structure title titleCRYSTAL STRUCTURE OF RAB GERANYLGERANYLTRANSFERASE FROM RAT BRAIN
Keywords keywordsRAB GERANYLGERANYLTRANSFERASE, 2.0 A RESOLUTION, N-FORMYLMETHIONINE, ALPHA SUBUNIT, BETA SUBUNIT, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.16
Radius of gyration Rg (electron density) rg_electron42.81
Forward intensity I(0) i0607054000.00
Molecular weight molecular_weight201580.0 kDa
Excluded volume excluded_volume251730 ų
Envelope volume envelope_volume336780 ų
Hydration-shell volume shell_volume65564 ų
Envelope diameter envelope_diameter139.6
Shell Rg shell_rg47.74
Envelope Rg envelope_rg42.11
Shape Rg shape_rg42.82
Total Rg total_rg43.03
Total atoms total_atoms14153
Residues n_residues1790
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 dmax142.6
Rg (real space) rg_real43.15
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real6.0710e+08
I(0) uncertainty (real space) i0_real_error1.0450e+07
Rg (reciprocal space) rg_reciprocal43.16
I(0) (reciprocal space) i0_reciprocal607100000.0000
Solution quality estimate total_estimate0.8973
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.2
Skewness Skewness skewness0.278
Kurtosis Kurtosis kurtosis-0.607
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha89960000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.949

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd1dcea1
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_idd1dcea2
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_idd1dcea3
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_idd1dceb_
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_idd1dcec1
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_idd1dcec2
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_idd1dcec3
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_idd1dced_
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 (8 domains)

Domain ID domain_id1dceA01
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_id1dceA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1130 — Rab geranylgeranyltransferase alpha-subunit, insert domain
Domain ID domain_id1dceA03
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_id1dceB00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id1dceC01
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_id1dceC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1130 — Rab geranylgeranyltransferase alpha-subunit, insert domain
Domain ID domain_id1dceC03
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_id1dceD00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)