4d0m

Phosphatidylinositol 4-kinase III beta in a complex with Rab11a-GTP- gamma-S and the Rab-binding domain of FIP3

Method: X-RAY DIFFRACTION Dmax: 206.1 Å Quality: REASONABLE

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

PHOSPHATIDYLINOSITOL 4-KINASE BETA

HOMO SAPIENS

UniProt Q9UBF8

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 121–303 Chain A; UniProt 319–421 Chain A; UniProt 522–799 Chain C; UniProt 121–303 Chain C; UniProt 319–421 Chain C; UniProt 522–799 Chain O; UniProt 121–303 Chain O; UniProt 319–421 Chain O; UniProt 522–799 Chain S; UniProt 121–303 Chain S; UniProt 319–421 Chain S; UniProt 522–799 Mutation:YES RAS-RELATED PROTEIN RAB-11A × 4 (P62491) RAB11 FAMILY-INTERACTING PROTEIN 3 × 4 (O75154) 093 N-(5-(4-CHLORO-3-(2-HYDROXY-ETHYLSULFAMOYL)- PHENYLTHIAZOLE-2-YL)-ACETAMIDE × 4 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 4 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:16% PEG 6K, 0.01 M NA CITRATE Resolution 6.00 Å R-free 0.359
2 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain G; UniProt 121–303 Chain G; UniProt 319–421 Chain G; UniProt 522–799 Chain I; UniProt 121–303 Chain I; UniProt 319–421 Chain I; UniProt 522–799 Chain M; UniProt 121–303 Chain M; UniProt 319–421 Chain M; UniProt 522–799 Chain Q; UniProt 121–303 Chain Q; UniProt 319–421 Chain Q; UniProt 522–799 Mutation:YES RAS-RELATED PROTEIN RAB-11A × 4 (P62491) RAB11 FAMILY-INTERACTING PROTEIN 3 × 4 (O75154) 093 N-(5-(4-CHLORO-3-(2-HYDROXY-ETHYLSULFAMOYL)- PHENYLTHIAZOLE-2-YL)-ACETAMIDE × 4 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 4 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:16% PEG 6K, 0.01 M NA CITRATE Resolution 6.00 Å R-free 0.359
3 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain W; UniProt 121–303 Chain W; UniProt 319–421 Chain W; UniProt 522–799 Chain Y; UniProt 121–303 Chain Y; UniProt 319–421 Chain Y; UniProt 522–799 Chain c; UniProt 121–303 Chain c; UniProt 319–421 Chain c; UniProt 522–799 Chain g; UniProt 121–303 Chain g; UniProt 319–421 Chain g; UniProt 522–799 Mutation:YES RAS-RELATED PROTEIN RAB-11A × 4 (P62491) RAB11 FAMILY-INTERACTING PROTEIN 3 × 4 (O75154) 093 N-(5-(4-CHLORO-3-(2-HYDROXY-ETHYLSULFAMOYL)- PHENYLTHIAZOLE-2-YL)-ACETAMIDE × 4 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 4 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:16% PEG 6K, 0.01 M NA CITRATE Resolution 6.00 Å R-free 0.359

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.

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

View Construct and Data Evidence
UniProt name PI4KB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–185; UniProt 121–303 Author chain A; PDBConstruct 186–288; UniProt 319–421 Author chain A; PDBConstruct 289–566; UniProt 522–799 Author chain C; PDBConstruct 3–185; UniProt 121–303 Author chain C; PDBConstruct 186–288; UniProt 319–421 Author chain C; PDBConstruct 289–566; UniProt 522–799 Author chain G; PDBConstruct 3–185; UniProt 121–303 Author chain G; PDBConstruct 186–288; UniProt 319–421 Author chain G; PDBConstruct 289–566; UniProt 522–799 Author chain I; PDBConstruct 3–185; UniProt 121–303 Author chain I; PDBConstruct 186–288; UniProt 319–421 Author chain I; PDBConstruct 289–566; UniProt 522–799 Author chain M; PDBConstruct 3–185; UniProt 121–303 Author chain M; PDBConstruct 186–288; UniProt 319–421 Author chain M; PDBConstruct 289–566; UniProt 522–799 Author chain O; PDBConstruct 3–185; UniProt 121–303 Author chain O; PDBConstruct 186–288; UniProt 319–421 Author chain O; PDBConstruct 289–566; UniProt 522–799 Author chain Q; PDBConstruct 3–185; UniProt 121–303 Author chain Q; PDBConstruct 186–288; UniProt 319–421 Author chain Q; PDBConstruct 289–566; UniProt 522–799 Author chain S; PDBConstruct 3–185; UniProt 121–303 Author chain S; PDBConstruct 186–288; UniProt 319–421 Author chain S; PDBConstruct 289–566; UniProt 522–799 Author chain W; PDBConstruct 3–185; UniProt 121–303 Author chain W; PDBConstruct 186–288; UniProt 319–421 Author chain W; PDBConstruct 289–566; UniProt 522–799 Author chain Y; PDBConstruct 3–185; UniProt 121–303 Author chain Y; PDBConstruct 186–288; UniProt 319–421 Author chain Y; PDBConstruct 289–566; UniProt 522–799 Author chain c; PDBConstruct 3–185; UniProt 121–303 Author chain c; PDBConstruct 186–288; UniProt 319–421 Author chain c; PDBConstruct 289–566; UniProt 522–799 Author chain g; PDBConstruct 3–185; UniProt 121–303 Author chain g; PDBConstruct 186–288; UniProt 319–421 Author chain g; PDBConstruct 289–566; UniProt 522–799

RAS-RELATED PROTEIN RAB-11A

HOMO SAPIENS

UniProt P62491

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 1–216 Chain D; UniProt 1–216 Chain P; UniProt 1–216 Chain T; UniProt 1–216 Mutation:YES PHOSPHATIDYLINOSITOL 4-KINASE BETA × 4 (Q9UBF8) RAB11 FAMILY-INTERACTING PROTEIN 3 × 4 (O75154) 093 N-(5-(4-CHLORO-3-(2-HYDROXY-ETHYLSULFAMOYL)- PHENYLTHIAZOLE-2-YL)-ACETAMIDE × 4 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 4 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:16% PEG 6K, 0.01 M NA CITRATE Resolution 6.00 Å R-free 0.359
2 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain H; UniProt 1–216 Chain J; UniProt 1–216 Chain N; UniProt 1–216 Chain R; UniProt 1–216 Mutation:YES PHOSPHATIDYLINOSITOL 4-KINASE BETA × 4 (Q9UBF8) RAB11 FAMILY-INTERACTING PROTEIN 3 × 4 (O75154) 093 N-(5-(4-CHLORO-3-(2-HYDROXY-ETHYLSULFAMOYL)- PHENYLTHIAZOLE-2-YL)-ACETAMIDE × 4 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 4 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:16% PEG 6K, 0.01 M NA CITRATE Resolution 6.00 Å R-free 0.359
3 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain X; UniProt 1–216 Chain Z; UniProt 1–216 Chain d; UniProt 1–216 Chain h; UniProt 1–216 Mutation:YES PHOSPHATIDYLINOSITOL 4-KINASE BETA × 4 (Q9UBF8) RAB11 FAMILY-INTERACTING PROTEIN 3 × 4 (O75154) 093 N-(5-(4-CHLORO-3-(2-HYDROXY-ETHYLSULFAMOYL)- PHENYLTHIAZOLE-2-YL)-ACETAMIDE × 4 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 4 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:16% PEG 6K, 0.01 M NA CITRATE Resolution 6.00 Å R-free 0.359

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.

26 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RB11A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–219; UniProt 1–216 Author chain D; PDBConstruct 4–219; UniProt 1–216 Author chain H; PDBConstruct 4–219; UniProt 1–216 Author chain J; PDBConstruct 4–219; UniProt 1–216 Author chain N; PDBConstruct 4–219; UniProt 1–216 Author chain P; PDBConstruct 4–219; UniProt 1–216 Author chain R; PDBConstruct 4–219; UniProt 1–216 Author chain T; PDBConstruct 4–219; UniProt 1–216 Author chain X; PDBConstruct 4–219; UniProt 1–216 Author chain Z; PDBConstruct 4–219; UniProt 1–216 Author chain d; PDBConstruct 4–219; UniProt 1–216 Author chain h; PDBConstruct 4–219; UniProt 1–216

RAB11 FAMILY-INTERACTING PROTEIN 3

HOMO SAPIENS

UniProt O75154

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain E; UniProt 713–756 Chain F; UniProt 713–756 Chain U; UniProt 713–756 Chain V; UniProt 713–756 Fragment:RAB-BINDING DOMAIN Mutation:YES PHOSPHATIDYLINOSITOL 4-KINASE BETA × 4 (Q9UBF8) RAS-RELATED PROTEIN RAB-11A × 4 (P62491) 093 N-(5-(4-CHLORO-3-(2-HYDROXY-ETHYLSULFAMOYL)- PHENYLTHIAZOLE-2-YL)-ACETAMIDE × 4 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 4 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:16% PEG 6K, 0.01 M NA CITRATE Resolution 6.00 Å R-free 0.359
2 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain K; UniProt 713–756 Chain L; UniProt 713–756 Chain e; UniProt 713–756 Chain f; UniProt 713–756 Fragment:RAB-BINDING DOMAIN Mutation:YES PHOSPHATIDYLINOSITOL 4-KINASE BETA × 4 (Q9UBF8) RAS-RELATED PROTEIN RAB-11A × 4 (P62491) 093 N-(5-(4-CHLORO-3-(2-HYDROXY-ETHYLSULFAMOYL)- PHENYLTHIAZOLE-2-YL)-ACETAMIDE × 4 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 4 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:16% PEG 6K, 0.01 M NA CITRATE Resolution 6.00 Å R-free 0.359
3 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain a; UniProt 713–756 Chain b; UniProt 713–756 Chain i; UniProt 713–756 Chain j; UniProt 713–756 Fragment:RAB-BINDING DOMAIN Mutation:YES PHOSPHATIDYLINOSITOL 4-KINASE BETA × 4 (Q9UBF8) RAS-RELATED PROTEIN RAB-11A × 4 (P62491) 093 N-(5-(4-CHLORO-3-(2-HYDROXY-ETHYLSULFAMOYL)- PHENYLTHIAZOLE-2-YL)-ACETAMIDE × 4 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 4 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:16% PEG 6K, 0.01 M NA CITRATE Resolution 6.00 Å R-free 0.359

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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFIP3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 5–48; UniProt 713–756 Author chain F; PDBConstruct 5–48; UniProt 713–756 Author chain K; PDBConstruct 5–48; UniProt 713–756 Author chain L; PDBConstruct 5–48; UniProt 713–756 Author chain U; PDBConstruct 5–48; UniProt 713–756 Author chain V; PDBConstruct 5–48; UniProt 713–756 Author chain a; PDBConstruct 5–48; UniProt 713–756 Author chain b; PDBConstruct 5–48; UniProt 713–756 Author chain e; PDBConstruct 5–48; UniProt 713–756 Author chain f; PDBConstruct 5–48; UniProt 713–756 Author chain i; PDBConstruct 5–48; UniProt 713–756 Author chain j; PDBConstruct 5–48; UniProt 713–756

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 4d0m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4d0m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4d0m
Deposition date deposition_date2014-04-29
Structure title titlePhosphatidylinositol 4-kinase III beta in a complex with Rab11a-GTP- gamma-S and the Rab-binding domain of FIP3
Keywords keywords;PHOSPHOINOSITIDE, PHOSPHATIDYLINOSITOL 4-KINASE, LIPID KINASE, FAMILY OF RAB INTERACTING PROTEINS, FIP3, RAB-BINDING DOMAIN, RBD, RAB11, GTP, PIK93, GOLGI, RECYCLING ENDOSOME, 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_guinier84.85
Radius of gyration Rg (electron density) rg_electron84.56
Forward intensity I(0) i024067000000.00
Molecular weight molecular_weight871670.0 kDa
Excluded volume excluded_volume842170 ų
Envelope volume envelope_volume1987500 ų
Hydration-shell volume shell_volume192660 ų
Envelope diameter envelope_diameter273.4
Shell Rg shell_rg88.19
Envelope Rg envelope_rg80.11
Shape Rg shape_rg84.57
Total Rg total_rg84.55
Total atoms total_atoms65970
Residues n_residues8154
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 dmax206.1
Rg (real space) rg_real82.21
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real2.3110e+10
I(0) uncertainty (real space) i0_real_error3.2630e+08
Rg (reciprocal space) rg_reciprocal85.33
I(0) (reciprocal space) i0_reciprocal24100000000.0000
Solution quality estimate total_estimate0.6304
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary137.4
Skewness Skewness skewness-0.020
Kurtosis Kurtosis kurtosis-0.950
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.6654
Highest regularization parameter α highest_alpha1823000000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.999; Stabil: 0.970; Sysdev: 0.000; Positv: 1.000; Valcen: 0.309; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)