6pai

Structure of the human DDB1-DDA1-DCAF15 E3 ubiquitin ligase bound to RBM39 and sulfonamide E7820

Method: X-RAY DIFFRACTION Dmax: 136.4 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1140 Not recorded DDB1- and CUL4-associated factor 15 × 1 (Q66K64) RNA-binding protein 39 × 1 (Q7Z3L0) DET1- and DDB1-associated protein 1 × 1 (Q9BW61) EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 O6M 3-cyano-N-(3-cyano-4-methyl-1H-indol-7-yl)benzene-1-sulfonamide × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;0.1 M sodium HEPES, pH 7.0, 15% w/v PEG4000 Resolution 2.90 Å R-free 0.252

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 290 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 1–1140; UniProt 1–1140

DDB1- and CUL4-associated factor 15

Homo sapiens

UniProt Q66K64

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 2–275 Chain C; UniProt 384–600 Mutation:UNP residues 2-275,384-600 DNA damage-binding protein 1 × 1 (Q16531) RNA-binding protein 39 × 1 (Q7Z3L0) DET1- and DDB1-associated protein 1 × 1 (Q9BW61) EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 O6M 3-cyano-N-(3-cyano-4-methyl-1H-indol-7-yl)benzene-1-sulfonamide × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;0.1 M sodium HEPES, pH 7.0, 15% w/v PEG4000 Resolution 2.90 Å R-free 0.252

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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DCA15_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 8–281; UniProt 2–275 Author chain C; PDBConstruct 282–498; UniProt 384–600

RNA-binding protein 39

Homo sapiens

UniProt Q7Z3L0

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 78–174 Not recorded DNA damage-binding protein 1 × 1 (Q16531) DDB1- and CUL4-associated factor 15 × 1 (Q66K64) DET1- and DDB1-associated protein 1 × 1 (Q9BW61) EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 O6M 3-cyano-N-(3-cyano-4-methyl-1H-indol-7-yl)benzene-1-sulfonamide × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;0.1 M sodium HEPES, pH 7.0, 15% w/v PEG4000 Resolution 2.90 Å R-free 0.252

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q7Z3L0_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 5–101; UniProt 78–174

DET1- and DDB1-associated protein 1

Homo sapiens

UniProt Q9BW61

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–102 Not recorded DNA damage-binding protein 1 × 1 (Q16531) DDB1- and CUL4-associated factor 15 × 1 (Q66K64) RNA-binding protein 39 × 1 (Q7Z3L0) EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 O6M 3-cyano-N-(3-cyano-4-methyl-1H-indol-7-yl)benzene-1-sulfonamide × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;0.1 M sodium HEPES, pH 7.0, 15% w/v PEG4000 Resolution 2.90 Å R-free 0.252

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.

29 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DDA1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–102; UniProt 1–102

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 6pai

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6pai
Deposition date deposition_date2019-06-11
Structure title titleStructure of the human DDB1-DDA1-DCAF15 E3 ubiquitin ligase bound to RBM39 and sulfonamide E7820
Keywords keywordssulfonamide, RBM39, DCAF15, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.59
Radius of gyration Rg (electron density) rg_electron39.26
Forward intensity I(0) i0510396000.00
Molecular weight molecular_weight186850.0 kDa
Excluded volume excluded_volume234970 ų
Envelope volume envelope_volume310300 ų
Hydration-shell volume shell_volume65733 ų
Envelope diameter envelope_diameter147.9
Shell Rg shell_rg44.84
Envelope Rg envelope_rg39.24
Shape Rg shape_rg39.27
Total Rg total_rg39.53
Total atoms total_atoms13142
Residues n_residues1649
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 dmax136.4
Rg (real space) rg_real39.67
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real5.1040e+08
I(0) uncertainty (real space) i0_real_error9.3060e+06
Rg (reciprocal space) rg_reciprocal39.62
I(0) (reciprocal space) i0_reciprocal510400000.0000
Solution quality estimate total_estimate0.8540
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary133.0
Skewness Skewness skewness0.469
Kurtosis Kurtosis kurtosis-0.032
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha157500000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.766; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.807

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6paid_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family familyd.58.7.0 — automated matches

CATH v4.4 (3 domains)

Domain ID domain_id6paiA01
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_id6paiA02
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_id6paiD00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain

8. Citations (2)

9. Files and Curves (10)