2n73

Solution structure of the ACBD3:PI4KB complex

Method: SOLUTION NMR Dmax: 63.6 Å Quality: REASONABLE

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

Golgi resident protein GCP60

Homo sapiens

UniProt Q9H3P7

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 241–308 Fragment:UNP residues 241-308 Phosphatidylinositol 4-kinase beta × 1 (A0A0B4J1S8) SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 0.1;Pressure ambient NMR sample composition:0.47 mM [U-13C; U-15N] protein_1, 0.47 mM [U-13C; U-15N] protein_2, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

11 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCP60_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–69; UniProt 241–308

Phosphatidylinositol 4-kinase beta

Homo sapiens

UniProt A0A0B4J1S8

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 5–80 Fragment:UNP residues 5-80 Golgi resident protein GCP60 × 1 (Q9H3P7) SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 0.1;Pressure ambient NMR sample composition:0.47 mM [U-13C; U-15N] protein_1, 0.47 mM [U-13C; U-15N] protein_2, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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 A0A0B4J1S8_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–80; UniProt 5–80

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 2n73

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2n73
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2n73
Deposition date deposition_date2015-09-02
Structure title titleSolution structure of the ACBD3:PI4KB complex
Keywords keywordskinase, TRANSFERASE-TRANSFERASE REGULATOR complex; TRANSFERASE/TRANSFERASE REGULATOR
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier31.84
Radius of gyration Rg (electron density) rg_electron32.85
Forward intensity I(0) i07816160000.00
Molecular weight molecular_weight733030.0 kDa
Excluded volume excluded_volume911190 ų
Envelope volume envelope_volume547030 ų
Hydration-shell volume shell_volume85333 ų
Envelope diameter envelope_diameter168.5
Shell Rg shell_rg55.60
Envelope Rg envelope_rg52.78
Shape Rg shape_rg32.79
Total Rg total_rg33.40
Total atoms total_atoms102735
Residues n_residues6705
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 dmax63.6
Rg (real space) rg_real22.47
Rg uncertainty (real space) rg_real_error0.11
I(0) (real space) i0_real6.1780e+09
I(0) uncertainty (real space) i0_real_error5.6810e+07
Rg (reciprocal space) rg_reciprocal32.48
I(0) (reciprocal space) i0_reciprocal7813000000.0000
Solution quality estimate total_estimate0.5620
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.359
Kurtosis Kurtosis kurtosis-0.822
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha8.5470
Highest regularization parameter α highest_alpha223700.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.967; Stabil: 0.908; Sysdev: 0.000; Positv: 1.000; Valcen: 0.678; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)