4ont

Ternary host recognition complex of complement factor H, C3d, and sialic acid

Method: X-RAY DIFFRACTION Dmax: 132.8 Å Quality: REASONABLE

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

Complement factor H

Homo sapiens

UniProt P08603

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 1107–1231 Fragment:Sushi 19-20 domains (UNP residues 1107-1231) Complement C3d fragment × 1 (P01024) N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;293 K;0.1 M Tris-HCl, pH 9.0, 8% w/v PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.15 Å R-free 0.223
2 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1107–1231 Fragment:Sushi 19-20 domains (UNP residues 1107-1231) Complement C3d fragment × 1 (P01024) N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;293 K;0.1 M Tris-HCl, pH 9.0, 8% w/v PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.15 Å R-free 0.223
3 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1107–1231 Fragment:Sushi 19-20 domains (UNP residues 1107-1231) Complement C3d fragment × 1 (P01024) N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;293 K;0.1 M Tris-HCl, pH 9.0, 8% w/v PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.15 Å R-free 0.223

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.

47 other PDB entries and 73 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CFAH_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 5–129; UniProt 1107–1231 Author chain E; PDBConstruct 5–129; UniProt 1107–1231 Author chain F; PDBConstruct 5–129; UniProt 1107–1231

Complement C3d fragment

Homo sapiens

UniProt P01024

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 996–1303 Fragment:UNP residues 996-1303 Mutation:C17A Complement factor H × 1 (P08603) N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;293 K;0.1 M Tris-HCl, pH 9.0, 8% w/v PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.15 Å R-free 0.223
2 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 996–1303 Fragment:UNP residues 996-1303 Mutation:C17A Complement factor H × 1 (P08603) N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;293 K;0.1 M Tris-HCl, pH 9.0, 8% w/v PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.15 Å R-free 0.223
3 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 996–1303 Fragment:UNP residues 996-1303 Mutation:C17A Complement factor H × 1 (P08603) N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;293 K;0.1 M Tris-HCl, pH 9.0, 8% w/v PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.15 Å R-free 0.223

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.

74 other PDB entries and 115 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CO3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 10–317; UniProt 996–1303 Author chain B; PDBConstruct 10–317; UniProt 996–1303 Author chain C; PDBConstruct 10–317; UniProt 996–1303

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 4ont

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ont
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ont
Deposition date deposition_date2014-01-29
Structure title titleTernary host recognition complex of complement factor H, C3d, and sialic acid
Keywords keywords;complement control protein, CCP, short consensus repeat, SCR, sushi domain, complement regulation, sialic acid, host glycan, host cell surface, IMMUNE SYSTEM ;; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.63
Radius of gyration Rg (electron density) rg_electron39.19
Forward intensity I(0) i0296804000.00
Molecular weight molecular_weight141830.0 kDa
Excluded volume excluded_volume178190 ų
Envelope volume envelope_volume237270 ų
Hydration-shell volume shell_volume51840 ų
Envelope diameter envelope_diameter144.1
Shell Rg shell_rg43.28
Envelope Rg envelope_rg39.63
Shape Rg shape_rg39.18
Total Rg total_rg39.49
Total atoms total_atoms9978
Residues n_residues1255
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 dmax132.8
Rg (real space) rg_real39.65
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real2.9680e+08
I(0) uncertainty (real space) i0_real_error5.5820e+06
Rg (reciprocal space) rg_reciprocal39.64
I(0) (reciprocal space) i0_reciprocal296800000.0000
Solution quality estimate total_estimate0.6747
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.5
Skewness Skewness skewness0.295
Kurtosis Kurtosis kurtosis-0.454
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29390000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.906; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.977; Smooth: 0.884

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 13 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4onta1
Class classa — All alpha proteins
Fold Fold folda.102 — alpha/alpha toroid
Superfamily Superfamily superfamilya.102.4 — Terpenoid cyclases/Protein prenyltransferases
Family Family familya.102.4.4 — Complement components
Domain ID domain_idd4onta2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4ontb_
Class classa — All alpha proteins
Fold Fold folda.102 — alpha/alpha toroid
Superfamily Superfamily superfamilya.102.4 — Terpenoid cyclases/Protein prenyltransferases
Family Family familya.102.4.4 — Complement components
Domain ID domain_idd4ontc_
Class classa — All alpha proteins
Fold Fold folda.102 — alpha/alpha toroid
Superfamily Superfamily superfamilya.102.4 — Terpenoid cyclases/Protein prenyltransferases
Family Family familya.102.4.4 — Complement components

CATH v4.4 (9 domains)

Domain ID domain_id4ontA00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id4ontB00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id4ontC00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id4ontD01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id4ontD02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id4ontE01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id4ontE02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id4ontF01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id4ontF02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1

8. Citations (1)

9. Files and Curves (10)