7zn7

Cryo-EM structure of RCMV-E E27 bound to human DDB1 (deltaBPB) and rat STAT2 CCD

Method: ELECTRON MICROSCOPY Dmax: 121.4 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–396 Chain A; UniProt 706–1140 Mutation:delta396-705 GNGNSG B27a × 1 (K7Y9Z1) Signal transducer and activator of transcription × 1 (Q5XI26) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE;45 seconds adsorption 2 seconds blot Resolution 3.78 Å

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 4–399; UniProt 1–396 Author chain A; PDBConstruct 406–840; UniProt 706–1140

B27a

Murid betaherpesvirus 8

UniProt K7Y9Z1

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 1–656 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Signal transducer and activator of transcription × 1 (Q5XI26) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE;45 seconds adsorption 2 seconds blot Resolution 3.78 Å

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 K7Y9Z1_RCMVE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–659; UniProt 1–656

Signal transducer and activator of transcription

Rattus norvegicus

UniProt Q5XI26

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 D; UniProt 1–842 Not recorded DNA damage-binding protein 1 × 1 (Q16531) B27a × 1 (K7Y9Z1) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE;45 seconds adsorption 2 seconds blot Resolution 3.78 Å

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 Q5XI26_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 4–845; UniProt 1–842

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 7zn7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7zn7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7zn7
Deposition date deposition_date2022-04-20
Structure title titleCryo-EM structure of RCMV-E E27 bound to human DDB1 (deltaBPB) and rat STAT2 CCD
Keywords keywords;Interferon, ubiquitin-proteasome system, Cullin-RING ubiquitin ligases (CRL), DDB1, DCAFs, viral DCAF (vDCAF), cytomegalovirus, STAT2, IRF9, VIRUS ;; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.75
Radius of gyration Rg (electron density) rg_electron36.19
Forward intensity I(0) i0335378000.00
Molecular weight molecular_weight149400.0 kDa
Excluded volume excluded_volume187710 ų
Envelope volume envelope_volume252500 ų
Hydration-shell volume shell_volume57045 ų
Envelope diameter envelope_diameter125.0
Shell Rg shell_rg43.07
Envelope Rg envelope_rg36.45
Shape Rg shape_rg36.19
Total Rg total_rg36.65
Total atoms total_atoms10497
Residues n_residues1311
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 dmax121.4
Rg (real space) rg_real36.68
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real3.3540e+08
I(0) uncertainty (real space) i0_real_error5.5750e+06
Rg (reciprocal space) rg_reciprocal36.73
I(0) (reciprocal space) i0_reciprocal335400000.0000
Solution quality estimate total_estimate0.8870
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.2
Skewness Skewness skewness0.297
Kurtosis Kurtosis kurtosis-0.347
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha70140000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.864; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.937

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7zn7A01
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_id7zn7A02
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_id7zn7A03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily910

8. Citations (1)

9. Files and Curves (10)