6y0a

CRYSTAL STRUCTURE OF CDK8-CycC IN COMPLEX WITH BI00690300

Method: X-RAY DIFFRACTION Dmax: 90.2 Å Quality: EXCELLENT

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

Cyclin-dependent kinase 8

Homo sapiens

UniProt P49336

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 1–403 Not recorded Cyclin-C × 1 (P24863) JRE 6-[5-chloranyl-4-[(1~{S})-1-oxidanylethyl]pyridin-3-yl]-3,4-dihydro-2~{H}-1,8-naphthyridine-1-carboxamide × 1 EDO 1,2-ETHANEDIOL × 1 FMT FORMIC ACID × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;298 K;20% (wt/vol) polyethylene glycol 3350 0.2 M sodium formate Resolution 2.19 Å R-free 0.227

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.

35 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDK8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–406; UniProt 1–403

Cyclin-C

Homo sapiens

UniProt P24863

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 1–280 Not recorded Cyclin-dependent kinase 8 × 1 (P49336) JRE 6-[5-chloranyl-4-[(1~{S})-1-oxidanylethyl]pyridin-3-yl]-3,4-dihydro-2~{H}-1,8-naphthyridine-1-carboxamide × 1 EDO 1,2-ETHANEDIOL × 1 FMT FORMIC ACID × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;298 K;20% (wt/vol) polyethylene glycol 3350 0.2 M sodium formate Resolution 2.19 Å R-free 0.227

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.

35 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCNC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–283; UniProt 1–280

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 6y0a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6y0a
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6y0a
Deposition date deposition_date2020-02-07
Structure title titleCRYSTAL STRUCTURE OF CDK8-CycC IN COMPLEX WITH BI00690300
Keywords keywordsVIENNA, KINASE, CELL CYCLE; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.09
Radius of gyration Rg (electron density) rg_electron28.14
Forward intensity I(0) i079614500.00
Molecular weight molecular_weight72666.0 kDa
Excluded volume excluded_volume92120 ų
Envelope volume envelope_volume114470 ų
Hydration-shell volume shell_volume33818 ų
Envelope diameter envelope_diameter95.5
Shell Rg shell_rg35.54
Envelope Rg envelope_rg28.24
Shape Rg shape_rg28.13
Total Rg total_rg28.95
Total atoms total_atoms5117
Residues n_residues613
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 dmax90.2
Rg (real space) rg_real29.06
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real7.9610e+07
I(0) uncertainty (real space) i0_real_error1.2030e+06
Rg (reciprocal space) rg_reciprocal29.08
I(0) (reciprocal space) i0_reciprocal79620000.0000
Solution quality estimate total_estimate0.9040
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.2
Skewness Skewness skewness0.277
Kurtosis Kurtosis kurtosis-0.553
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25270000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.893

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)