5fbq

PI4KB in complex with Rab11 and the MI358 Inhibitor

Method: X-RAY DIFFRACTION Dmax: 94.0 Å Quality: REASONABLE

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

Phosphatidylinositol 4-kinase beta,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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 128–422 Chain A; UniProt 523–799 Fragment:UNP Residues 128-422, 523-799 Ras-related protein Rab-11A × 1 (P62491) 5W6 ~{N}-[2-[[6-chloranyl-3-[3-[4-(hydroxymethyl)piperidin-1-yl]sulfonyl-4-methoxy-phenyl]-2-methyl-imidazo[1,2-b]pyridazin-8-yl]amino]ethyl]ethanamide × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2M magnesium chloride, 0.1M Tris PH=7, 10% (w/v) PEG 8000 Resolution 3.79 Å R-free 0.302

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 22 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 1–295; UniProt 128–422 Author chain A; PDBConstruct 296–572; UniProt 523–799

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–216 Not recorded Phosphatidylinositol 4-kinase beta,Phosphatidylinositol 4-kinase beta × 1 (Q9UBF8) 5W6 ~{N}-[2-[[6-chloranyl-3-[3-[4-(hydroxymethyl)piperidin-1-yl]sulfonyl-4-methoxy-phenyl]-2-methyl-imidazo[1,2-b]pyridazin-8-yl]amino]ethyl]ethanamide × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2M magnesium chloride, 0.1M Tris PH=7, 10% (w/v) PEG 8000 Resolution 3.79 Å R-free 0.302

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 58 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 6–221; UniProt 1–216

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 5fbq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5fbq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5fbq
Deposition date deposition_date2015-12-14
Structure title titlePI4KB in complex with Rab11 and the MI358 Inhibitor
Keywords keywordsInhibitor, Complex, Kinase, Lipid, Transferase; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.41
Radius of gyration Rg (electron density) rg_electron28.44
Forward intensity I(0) i080089400.00
Molecular weight molecular_weight71462.0 kDa
Excluded volume excluded_volume90054 ų
Envelope volume envelope_volume115730 ų
Hydration-shell volume shell_volume33878 ų
Envelope diameter envelope_diameter92.2
Shell Rg shell_rg35.84
Envelope Rg envelope_rg28.18
Shape Rg shape_rg28.45
Total Rg total_rg29.14
Total atoms total_atoms5039
Residues n_residues629
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 dmax94.0
Rg (real space) rg_real29.35
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real8.0090e+07
I(0) uncertainty (real space) i0_real_error1.0650e+06
Rg (reciprocal space) rg_reciprocal29.38
I(0) (reciprocal space) i0_reciprocal80090000.0000
Solution quality estimate total_estimate0.7251
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary92.3
Skewness Skewness skewness0.240
Kurtosis Kurtosis kurtosis-0.535
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21510000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 1.000; Sysdev: 0.218; Positv: 1.000; Valcen: 0.999; Smooth: 0.960

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id5fbqB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)