6o60

Crystal structure of GGTase3-FBXL2-SKP1 complex

Method: X-RAY DIFFRACTION Dmax: 124.0 Å Quality: GOOD

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

Protein prenyltransferase alpha subunit repeat-containing protein 1

Homo sapiens

UniProt Q7Z6K3

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 1–402 Not recorded Geranylgeranyl transferase type-2 subunit beta × 1 (P53611) F-box/LRR-repeat protein 2 × 1 (Q9UKC9) S-phase kinase-associated protein 1 × 1 (P63208) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M MES pH6.0, 20%-22% (v/v) PEG 400 Resolution 2.50 Å R-free 0.247

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTAR1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–407; UniProt 1–402

Geranylgeranyl transferase type-2 subunit beta

Homo sapiens

UniProt P53611

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 Protein prenyltransferase alpha subunit repeat-containing protein 1 × 1 (Q7Z6K3) F-box/LRR-repeat protein 2 × 1 (Q9UKC9) S-phase kinase-associated protein 1 × 1 (P63208) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M MES pH6.0, 20%-22% (v/v) PEG 400 Resolution 2.50 Å R-free 0.247

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PGTB2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–332; UniProt 1–331

F-box/LRR-repeat protein 2

Homo sapiens

UniProt Q9UKC9

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 C; UniProt 1–423 Not recorded Protein prenyltransferase alpha subunit repeat-containing protein 1 × 1 (Q7Z6K3) Geranylgeranyl transferase type-2 subunit beta × 1 (P53611) S-phase kinase-associated protein 1 × 1 (P63208) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M MES pH6.0, 20%-22% (v/v) PEG 400 Resolution 2.50 Å R-free 0.247

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 FBXL2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 2–424; UniProt 1–423

S-phase kinase-associated protein 1

Homo sapiens

UniProt P63208

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 D; UniProt 1–163 Not recorded Protein prenyltransferase alpha subunit repeat-containing protein 1 × 1 (Q7Z6K3) Geranylgeranyl transferase type-2 subunit beta × 1 (P53611) F-box/LRR-repeat protein 2 × 1 (Q9UKC9) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M MES pH6.0, 20%-22% (v/v) PEG 400 Resolution 2.50 Å R-free 0.247

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.

71 other PDB entries and 97 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SKP1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 2–164; UniProt 1–163

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 6o60

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6o60
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6o60
Deposition date deposition_date2019-03-04
Structure title titleCrystal structure of GGTase3-FBXL2-SKP1 complex
Keywords keywordsF-box, Leucine-rich repeat, GGTase subunits, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.67
Radius of gyration Rg (electron density) rg_electron34.94
Forward intensity I(0) i0267148000.00
Molecular weight molecular_weight131570.0 kDa
Excluded volume excluded_volume164690 ų
Envelope volume envelope_volume210300 ų
Hydration-shell volume shell_volume50018 ų
Envelope diameter envelope_diameter133.1
Shell Rg shell_rg41.61
Envelope Rg envelope_rg34.61
Shape Rg shape_rg34.94
Total Rg total_rg35.39
Total atoms total_atoms9229
Residues n_residues1157
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 dmax124.0
Rg (real space) rg_real35.61
Rg uncertainty (real space) rg_real_error1.02
I(0) (real space) i0_real2.6710e+08
I(0) uncertainty (real space) i0_real_error4.4840e+06
Rg (reciprocal space) rg_reciprocal35.65
I(0) (reciprocal space) i0_reciprocal267200000.0000
Solution quality estimate total_estimate0.8772
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.3
Skewness Skewness skewness0.284
Kurtosis Kurtosis kurtosis-0.369
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30040000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.807; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd6o60b_
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_idd6o60d1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.42 — POZ domain
Superfamily Superfamily superfamilyd.42.1 — POZ domain
Family Family familyd.42.1.0 — automated matches
Domain ID domain_idd6o60d2
Class classa — All alpha proteins
Fold Fold folda.157 — Skp1 dimerisation domain-like
Superfamily Superfamily superfamilya.157.1 — Skp1 dimerisation domain-like
Family Family familya.157.1.1 — Skp1 dimerisation domain-like

CATH v4.4 (2 domains)

Domain ID domain_id6o60B00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id6o60D00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology710 — Potassium Channel Kv1.1; Chain A
Homologous superfamily homologous superfamily10 — Potassium Channel Kv1.1; Chain A

8. Citations (1)

9. Files and Curves (10)