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6hga

Crystal Structure of the human IL-17RC D2-D3-D4 domains in complex with an anti-APP tag Fab

Method: X-RAY DIFFRACTION Dmax: 149.1 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Interleukin-17 receptor C

Homo sapiens

UniProt Q8NAC3

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 208–467 Fragment：IL-17RC D2-D3-D4 domains Mutation：N263Q,Q307R,N349Q,N372Q,N406Q anti-APP-tag Fab heavy-chain × 1 anti-APP-tag Fab light-chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；292 K；0.1M HEPES, 30% Jeffamine ED-2001 Resolution 2.60 Å R-free 0.232

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.

Other PDB Difference from Current Entry 6HGA Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6HG4 Crystal Structure of the human IL-17RC ECD in complex with human IL-17F Deposited 2018-08-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 21–467（447 aa）
Mutation：N186Q, N226Q, N253Q, N263Q, N349Q, N372Q, N406Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；200mM ammonium citrate tribasic, 20.0% PEG 3350
Resolution 3.32 Å R-free 0.239
6HG9 Crystal Structure of the human IL-17RC ECD in complex with human IL-17F, Crystal form II Deposited 2018-08-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 21–467（447 aa）
Mutation：N118Q, N186Q, N213Q, N226Q, N263Q, N349Q, Q307R, N372Q, N406Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；200mM ammonium formate, 20.0% PEG 3350
Resolution 3.62 Å R-free 0.258
7UWN Structure of the IL-17A-IL-17RA-IL-17RC ternary complex Deposited 2022-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 7 PDB declaration: heptameric
Chain G 21–465（445 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.01 Å
7ZAN Crystal Structure of human IL-17A in complex with IL-17RA and IL-17RC Deposited 2022-03-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain D 21–467（447 aa） Fragment：Extracellular domain
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1M MES, 10.0% PEG DME 500
Resolution 5.06 Å R-free 0.353

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

View Construct and Data Evidence
UniProt name I17RC_HUMAN
Isoform Q8NAC3-2
PDB entities 1
Chains and sequence ranges Author chain B； PDBConstruct 1–260； UniProt 208–467

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 6hga

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6hga
Deposition date deposition_date2018-08-23
Structure title titleCrystal Structure of the human IL-17RC D2-D3-D4 domains in complex with an anti-APP tag Fab
Keywords keywordsFnIII domains, Fab complex, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier41.41 Å
Radius of gyration Rg (electron density) rg_electron42.29 Å
Forward intensity I(0) i095872400.00
Molecular weight molecular_weight77829.0 kDa
Excluded volume excluded_volume97008 ų
Envelope volume envelope_volume141120 ų
Hydration-shell volume shell_volume31757 ų
Envelope diameter envelope_diameter157.9 Å
Shell Rg shell_rg40.03 Å
Envelope Rg envelope_rg43.45 Å
Shape Rg shape_rg42.31 Å
Total Rg total_rg42.11 Å
Total atoms total_atoms5477
Residues n_residues703
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax149.1 Å
Rg (real space) rg_real42.20 Å
Rg uncertainty (real space) rg_real_error2.20 Å
I(0) (real space) i0_real9.5870e+07
I(0) uncertainty (real space) i0_real_error1.9470e+06
Rg (reciprocal space) rg_reciprocal41.42 Å
I(0) (reciprocal space) i0_reciprocal95790000.0000
Solution quality estimate total_estimate0.7038
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.5 Å
Skewness Skewness skewness0.742
Kurtosis Kurtosis kurtosis-0.073
Angular range angular_range— – 0.1900 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5174000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.480; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.388; Smooth: 0.320
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd6hgah_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd6hgal1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd6hgal2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)

CATH v4.4 (2 domains)

Domain ID domain_id6hgaH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6hgaL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
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8. Citations (1)

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9. Files and Curves (10)