7jn7

Human DPP9-CARD8 complex

Method: ELECTRON MICROSCOPY Dmax: 142.9 Å Quality: GOOD

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

Dipeptidyl peptidase 9

Homo sapiens

UniProt Q86TI2

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 1–863 Chain D; UniProt 1–863 Not recorded Caspase recruitment domain-containing protein 8 × 2 (Q9Y2G2) GK2 [(2~{R})-1-[(2~{R})-2-azanyl-3-methyl-butanoyl]pyrrolidin-2-yl]boronic acid × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES, pH 7.5, 150 mM NaCl, 1 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

13 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPP9_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 29–891; UniProt 1–863 Author chain D; PDBConstruct 29–891; UniProt 1–863

Caspase recruitment domain-containing protein 8

Homo sapiens

UniProt Q9Y2G2

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 B; UniProt 1–537 Chain C; UniProt 1–537 Not recorded Dipeptidyl peptidase 9 × 2 (Q86TI2) GK2 [(2~{R})-1-[(2~{R})-2-azanyl-3-methyl-butanoyl]pyrrolidin-2-yl]boronic acid × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES, pH 7.5, 150 mM NaCl, 1 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CARD8_HUMAN
Isoform Q9Y2G2-5
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–537; UniProt 1–537 Author chain C; PDBConstruct 1–537; UniProt 1–537

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 7jn7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7jn7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7jn7
Deposition date deposition_date2020-08-04
Structure title titleHuman DPP9-CARD8 complex
Keywords keywordsCARD8, DPP9, inflammasome, Val-boroPro (VbP), talabostat, innate immunity, IMMUNE SYSTEM, HYDROLASE; IMMUNE SYSTEM, HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.27
Radius of gyration Rg (electron density) rg_electron42.96
Forward intensity I(0) i0764874000.00
Molecular weight molecular_weight232620.0 kDa
Excluded volume excluded_volume292340 ų
Envelope volume envelope_volume385500 ų
Hydration-shell volume shell_volume73192 ų
Envelope diameter envelope_diameter153.8
Shell Rg shell_rg49.17
Envelope Rg envelope_rg42.79
Shape Rg shape_rg42.95
Total Rg total_rg43.28
Total atoms total_atoms16455
Residues n_residues2044
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 dmax142.9
Rg (real space) rg_real43.22
Rg uncertainty (real space) rg_real_error1.65
I(0) (real space) i0_real7.6490e+08
I(0) uncertainty (real space) i0_real_error1.5530e+07
Rg (reciprocal space) rg_reciprocal43.27
I(0) (reciprocal space) i0_reciprocal764900000.0000
Solution quality estimate total_estimate0.8889
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.6
Skewness Skewness skewness0.283
Kurtosis Kurtosis kurtosis-0.454
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha136500000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.886

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7jn7A01
Class class2 — Mainly Beta
Architecture architecture140 — 8 Propeller
Topology topology10 — Methanol Dehydrogenase; Chain A
Homologous superfamily homologous superfamily30 — Dipeptidylpeptidase IV, N-terminal domain
Domain ID domain_id7jn7D01
Class class2 — Mainly Beta
Architecture architecture140 — 8 Propeller
Topology topology10 — Methanol Dehydrogenase; Chain A
Homologous superfamily homologous superfamily30 — Dipeptidylpeptidase IV, N-terminal domain

8. Citations (1)

9. Files and Curves (10)