7pw8

Human SMG1-8-9 kinase complex bound to AMPPNP

Method: ELECTRON MICROSCOPY Dmax: 171.3 Å Quality: GOOD

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

SMG1,Serine/threonine-protein kinase SMG1,SMG1,Serine/threonine-protein kinase SMG1,SMG1

Homo sapiens

UniProt Q96Q15

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 311–1638 Chain A; UniProt 1727–1978 Chain A; UniProt 1895–1916 Chain A; UniProt 2088–3661 Not recorded Protein SMG8 × 1 (Q8ND04) Protein SMG9 × 1 (Q9H0W8) IHP INOSITOL HEXAKISPHOSPHATE × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.82 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMG1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 307–1634; UniProt 311–1638 Author chain A; PDBConstruct 1723–1974; UniProt 1727–1978 Author chain A; PDBConstruct 2031–2052; UniProt 1895–1916 Author chain A; PDBConstruct 2084–3657; UniProt 2088–3661

Protein SMG8

Homo sapiens

UniProt Q8ND04

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 1–991 Not recorded SMG1,Serine/threonine-protein kinase SMG1,SMG1,Serine/threonine-protein kinase SMG1,SMG1 × 1 (Q96Q15) Protein SMG9 × 1 (Q9H0W8) IHP INOSITOL HEXAKISPHOSPHATE × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.82 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMG8_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–991; UniProt 1–991

Protein SMG9

Homo sapiens

UniProt Q9H0W8

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 1–520 Not recorded SMG1,Serine/threonine-protein kinase SMG1,SMG1,Serine/threonine-protein kinase SMG1,SMG1 × 1 (Q96Q15) Protein SMG8 × 1 (Q8ND04) IHP INOSITOL HEXAKISPHOSPHATE × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.82 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.

8 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMG9_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–520; UniProt 1–520

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 7pw8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7pw8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7pw8
Deposition date deposition_date2021-10-06
Structure title titleHuman SMG1-8-9 kinase complex bound to AMPPNP
Keywords keywordsComplex, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.88
Radius of gyration Rg (electron density) rg_electron49.21
Forward intensity I(0) i01013340000.00
Molecular weight molecular_weight268730.0 kDa
Excluded volume excluded_volume338040 ų
Envelope volume envelope_volume525420 ų
Hydration-shell volume shell_volume86927 ų
Envelope diameter envelope_diameter177.4
Shell Rg shell_rg54.24
Envelope Rg envelope_rg49.64
Shape Rg shape_rg49.30
Total Rg total_rg49.06
Total atoms total_atoms18960
Residues n_residues2629
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 dmax171.3
Rg (real space) rg_real49.94
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real1.0130e+09
I(0) uncertainty (real space) i0_real_error1.7400e+07
Rg (reciprocal space) rg_reciprocal49.89
I(0) (reciprocal space) i0_reciprocal1013000000.0000
Solution quality estimate total_estimate0.8774
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.9
Skewness Skewness skewness0.358
Kurtosis Kurtosis kurtosis-0.359
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha113700000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.840; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.886

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)