8bu4

Structure of DDB1 bound to DS22-engaged CDK12-cyclin K

Method: X-RAY DIFFRACTION Dmax: 175.2 Å Quality: GOOD

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

DNA damage-binding protein 1

Homo sapiens

UniProt Q16531

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 1–395 Chain A; UniProt 709–1140 Not recorded Cyclin-dependent kinase 12 × 1 (Q9NYV4) Cyclin-K × 1 (O75909) SO4 SULFATE ION × 5 RQL (2~{R})-2-[[6-[[5,6-bis(chloranyl)-1~{H}-benzimidazol-2-yl]methylamino]-9-(1-methylpyrazol-4-yl)purin-2-yl]amino]butan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.07 M ammonium sulfate, 0.855 M ammonium citrate, 0.07 M HEPES pH 7 Resolution 3.09 Å R-free 0.223
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–395 Chain D; UniProt 709–1140 Not recorded Cyclin-dependent kinase 12 × 1 (Q9NYV4) Cyclin-K × 1 (O75909) SO4 SULFATE ION × 6 RQL (2~{R})-2-[[6-[[5,6-bis(chloranyl)-1~{H}-benzimidazol-2-yl]methylamino]-9-(1-methylpyrazol-4-yl)purin-2-yl]amino]butan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.07 M ammonium sulfate, 0.855 M ammonium citrate, 0.07 M HEPES pH 7 Resolution 3.09 Å R-free 0.223
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 1–395 Chain G; UniProt 709–1140 Not recorded Cyclin-dependent kinase 12 × 1 (Q9NYV4) Cyclin-K × 1 (O75909) SO4 SULFATE ION × 3 RQL (2~{R})-2-[[6-[[5,6-bis(chloranyl)-1~{H}-benzimidazol-2-yl]methylamino]-9-(1-methylpyrazol-4-yl)purin-2-yl]amino]butan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.07 M ammonium sulfate, 0.855 M ammonium citrate, 0.07 M HEPES pH 7 Resolution 3.09 Å R-free 0.223

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.

202 other PDB entries and 288 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DDB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–399; UniProt 1–395 Author chain A; PDBConstruct 409–840; UniProt 709–1140 Author chain D; PDBConstruct 5–399; UniProt 1–395 Author chain D; PDBConstruct 409–840; UniProt 709–1140 Author chain G; PDBConstruct 5–399; UniProt 1–395 Author chain G; PDBConstruct 409–840; UniProt 709–1140

Cyclin-dependent kinase 12

Homo sapiens

UniProt Q9NYV4

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 712–1051 Non-standard monomer:Yes (specific site not provided by mmCIF) DNA damage-binding protein 1 × 1 (Q16531) Cyclin-K × 1 (O75909) SO4 SULFATE ION × 5 RQL (2~{R})-2-[[6-[[5,6-bis(chloranyl)-1~{H}-benzimidazol-2-yl]methylamino]-9-(1-methylpyrazol-4-yl)purin-2-yl]amino]butan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.07 M ammonium sulfate, 0.855 M ammonium citrate, 0.07 M HEPES pH 7 Resolution 3.09 Å R-free 0.223
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 712–1051 Non-standard monomer:Yes (specific site not provided by mmCIF) DNA damage-binding protein 1 × 1 (Q16531) Cyclin-K × 1 (O75909) SO4 SULFATE ION × 6 RQL (2~{R})-2-[[6-[[5,6-bis(chloranyl)-1~{H}-benzimidazol-2-yl]methylamino]-9-(1-methylpyrazol-4-yl)purin-2-yl]amino]butan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.07 M ammonium sulfate, 0.855 M ammonium citrate, 0.07 M HEPES pH 7 Resolution 3.09 Å R-free 0.223
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 712–1051 Non-standard monomer:Yes (specific site not provided by mmCIF) DNA damage-binding protein 1 × 1 (Q16531) Cyclin-K × 1 (O75909) SO4 SULFATE ION × 3 RQL (2~{R})-2-[[6-[[5,6-bis(chloranyl)-1~{H}-benzimidazol-2-yl]methylamino]-9-(1-methylpyrazol-4-yl)purin-2-yl]amino]butan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.07 M ammonium sulfate, 0.855 M ammonium citrate, 0.07 M HEPES pH 7 Resolution 3.09 Å R-free 0.223

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.

38 other PDB entries and 102 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDK12_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–343; UniProt 712–1051 Author chain E; PDBConstruct 4–343; UniProt 712–1051 Author chain H; PDBConstruct 4–343; UniProt 712–1051

Cyclin-K

Homo sapiens

UniProt O75909

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 1–267 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Cyclin-dependent kinase 12 × 1 (Q9NYV4) SO4 SULFATE ION × 5 RQL (2~{R})-2-[[6-[[5,6-bis(chloranyl)-1~{H}-benzimidazol-2-yl]methylamino]-9-(1-methylpyrazol-4-yl)purin-2-yl]amino]butan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.07 M ammonium sulfate, 0.855 M ammonium citrate, 0.07 M HEPES pH 7 Resolution 3.09 Å R-free 0.223
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 1–267 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Cyclin-dependent kinase 12 × 1 (Q9NYV4) SO4 SULFATE ION × 6 RQL (2~{R})-2-[[6-[[5,6-bis(chloranyl)-1~{H}-benzimidazol-2-yl]methylamino]-9-(1-methylpyrazol-4-yl)purin-2-yl]amino]butan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.07 M ammonium sulfate, 0.855 M ammonium citrate, 0.07 M HEPES pH 7 Resolution 3.09 Å R-free 0.223
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 1–267 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Cyclin-dependent kinase 12 × 1 (Q9NYV4) SO4 SULFATE ION × 3 RQL (2~{R})-2-[[6-[[5,6-bis(chloranyl)-1~{H}-benzimidazol-2-yl]methylamino]-9-(1-methylpyrazol-4-yl)purin-2-yl]amino]butan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.07 M ammonium sulfate, 0.855 M ammonium citrate, 0.07 M HEPES pH 7 Resolution 3.09 Å R-free 0.223

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.

40 other PDB entries and 105 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCNK_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 5–271; UniProt 1–267 Author chain F; PDBConstruct 5–271; UniProt 1–267 Author chain I; PDBConstruct 5–271; UniProt 1–267

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 8bu4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8bu4
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8bu4
Deposition date deposition_date2022-11-30
Structure title titleStructure of DDB1 bound to DS22-engaged CDK12-cyclin K
Keywords keywordskinase, cyclin, ubiquitin, degrader, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier63.49
Radius of gyration Rg (electron density) rg_electron63.02
Forward intensity I(0) i03171290000.00
Molecular weight molecular_weight481840.0 kDa
Excluded volume excluded_volume604930 ų
Envelope volume envelope_volume939140 ų
Hydration-shell volume shell_volume119280 ų
Envelope diameter envelope_diameter187.9
Shell Rg shell_rg71.40
Envelope Rg envelope_rg60.06
Shape Rg shape_rg63.00
Total Rg total_rg63.25
Total atoms total_atoms67490
Residues n_residues4204
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 dmax175.2
Rg (real space) rg_real63.14
Rg uncertainty (real space) rg_real_error1.41
I(0) (real space) i0_real3.1710e+09
I(0) uncertainty (real space) i0_real_error6.6660e+07
Rg (reciprocal space) rg_reciprocal63.73
I(0) (reciprocal space) i0_reciprocal3174000000.0000
Solution quality estimate total_estimate0.8453
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary98.1
Skewness Skewness skewness-0.012
Kurtosis Kurtosis kurtosis-0.839
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha328200000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.998; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 15 domains

CATH v4.4 (15 domains)

Domain ID domain_id8bu4A01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8bu4A02
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8bu4A03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily910
Domain ID domain_id8bu4B01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id8bu4B02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id8bu4D01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8bu4D02
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8bu4D03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily910
Domain ID domain_id8bu4E01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id8bu4E02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id8bu4G01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8bu4G02
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8bu4G03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily910
Domain ID domain_id8bu4H01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id8bu4H02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1

8. Citations (1)

9. Files and Curves (10)