6d0y

X-ray Crystal Structure of PGC-1beta C-terminus bound to the CBP80-CBP20 Cap Binding Complex

Method: X-RAY DIFFRACTION Dmax: 102.8 Å Quality: GOOD

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

Nuclear cap-binding protein subunit 1

Homo sapiens

UniProt Q09161

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 24–790 Not recorded Nuclear cap-binding protein subunit 2 × 1 (P52298) Peroxisome proliferator-activated receptor gamma coactivator 1-beta × 1 (Q86YN6) MG MAGNESIUM ION × 1 GTA P1-7-METHYLGUANOSINE-P3-ADENOSINE-5',5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;0.2 M magnesium chloride, 0.1 M Tris (pH 7.0), 10% [w/v] polyethylene glycol 8000 Resolution 2.68 Å R-free 0.240

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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NCBP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 2–768; UniProt 24–790

Nuclear cap-binding protein subunit 2

Homo sapiens

UniProt P52298

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–156 Not recorded Nuclear cap-binding protein subunit 1 × 1 (Q09161) Peroxisome proliferator-activated receptor gamma coactivator 1-beta × 1 (Q86YN6) MG MAGNESIUM ION × 1 GTA P1-7-METHYLGUANOSINE-P3-ADENOSINE-5',5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;0.2 M magnesium chloride, 0.1 M Tris (pH 7.0), 10% [w/v] polyethylene glycol 8000 Resolution 2.68 Å R-free 0.240

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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NCBP2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 21–176; UniProt 1–156

Peroxisome proliferator-activated receptor gamma coactivator 1-beta

OrganismNot specified

UniProt Q86YN6

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 955–984 Non-standard monomer:Yes (specific site not provided by mmCIF) Nuclear cap-binding protein subunit 1 × 1 (Q09161) Nuclear cap-binding protein subunit 2 × 1 (P52298) MG MAGNESIUM ION × 1 GTA P1-7-METHYLGUANOSINE-P3-ADENOSINE-5',5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;0.2 M magnesium chloride, 0.1 M Tris (pH 7.0), 10% [w/v] polyethylene glycol 8000 Resolution 2.68 Å R-free 0.240

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRGC2_HUMAN
Isoform Q86YN6-5
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 2–31; UniProt 955–984

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 6d0y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6d0y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6d0y
Deposition date deposition_date2018-04-11
Structure title titleX-ray Crystal Structure of PGC-1beta C-terminus bound to the CBP80-CBP20 Cap Binding Complex
Keywords keywordsCap-binding, m7GpppA, transcription, mRNA; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.64
Radius of gyration Rg (electron density) rg_electron30.60
Forward intensity I(0) i0170888000.00
Molecular weight molecular_weight104850.0 kDa
Excluded volume excluded_volume131460 ų
Envelope volume envelope_volume165400 ų
Hydration-shell volume shell_volume44083 ų
Envelope diameter envelope_diameter107.7
Shell Rg shell_rg38.54
Envelope Rg envelope_rg30.47
Shape Rg shape_rg30.58
Total Rg total_rg31.33
Total atoms total_atoms14475
Residues n_residues901
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 dmax102.8
Rg (real space) rg_real31.51
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real1.7090e+08
I(0) uncertainty (real space) i0_real_error2.9550e+06
Rg (reciprocal space) rg_reciprocal31.57
I(0) (reciprocal space) i0_reciprocal170900000.0000
Solution quality estimate total_estimate0.8899
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.1
Skewness Skewness skewness0.230
Kurtosis Kurtosis kurtosis-0.349
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha31800000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.948

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id6d0yA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain
Domain ID domain_id6d0yC01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180
Domain ID domain_id6d0yC02
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180
Domain ID domain_id6d0yC03
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180

8. Citations (1)

9. Files and Curves (10)