5nbq

The structure of the tripartite complex between OspE, the C-terminal domains of factor H and C3dg

Method: X-RAY DIFFRACTION Dmax: 137.7 Å Quality: GOOD

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

Complement C3

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 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 994–1287 Mutation:A1153E, C1010A Complement factor H × 1 (P08603) Outer surface protein E × 1 (Q45001) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;20% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 24% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 16% PEG3350, Tris pH 8.5, 0.2 M ammonium acetate Resolution 3.18 Å R-free 0.261
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 994–1287 Mutation:A1153E, C1010A Complement factor H × 1 (P08603) Outer surface protein E,Outer surface protein E × 1 (Q45001) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;20% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 24% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 16% PEG3350, Tris pH 8.5, 0.2 M ammonium acetate Resolution 3.18 Å R-free 0.261
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 994–1287 Mutation:A1153E, C1010A Complement factor H × 1 (P08603) Outer surface protein E × 1 (Q45001) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;20% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 24% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 16% PEG3350, Tris pH 8.5, 0.2 M ammonium acetate Resolution 3.18 Å R-free 0.261

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–294; UniProt 994–1287 Author chain B; PDBConstruct 1–294; UniProt 994–1287 Author chain C; PDBConstruct 1–294; UniProt 994–1287

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 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1104–1230 Not recorded Complement C3 × 1 (P01024) Outer surface protein E × 1 (Q45001) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;20% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 24% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 16% PEG3350, Tris pH 8.5, 0.2 M ammonium acetate Resolution 3.18 Å R-free 0.261
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1104–1230 Not recorded Complement C3 × 1 (P01024) Outer surface protein E,Outer surface protein E × 1 (Q45001) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;20% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 24% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 16% PEG3350, Tris pH 8.5, 0.2 M ammonium acetate Resolution 3.18 Å R-free 0.261
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 1104–1230 Not recorded Complement C3 × 1 (P01024) Outer surface protein E × 1 (Q45001) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;20% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 24% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 16% PEG3350, Tris pH 8.5, 0.2 M ammonium acetate Resolution 3.18 Å R-free 0.261

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 2
Chains and sequence ranges Author chain D; PDBConstruct 1–127; UniProt 1104–1230 Author chain E; PDBConstruct 1–127; UniProt 1104–1230 Author chain F; PDBConstruct 1–127; UniProt 1104–1230

Outer surface protein E

Borreliella burgdorferi

UniProt Q45001

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 G; UniProt 42–170 Not recorded Complement C3 × 1 (P01024) Complement factor H × 1 (P08603) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;20% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 24% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 16% PEG3350, Tris pH 8.5, 0.2 M ammonium acetate Resolution 3.18 Å R-free 0.261
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 42–170 Not recorded Complement C3 × 1 (P01024) Complement factor H × 1 (P08603) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;20% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 24% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 16% PEG3350, Tris pH 8.5, 0.2 M ammonium acetate Resolution 3.18 Å R-free 0.261
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 42–170 Not recorded Complement C3 × 1 (P01024) Complement factor H × 1 (P08603) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;20% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 24% PEG3350, 0.1 M HEPES pH 7.5, 0.2 M MgCl2 or 16% PEG3350, Tris pH 8.5, 0.2 M ammonium acetate Resolution 3.18 Å R-free 0.261

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q45001_BORBG
Isoform
PDB entities 3, 4
Chains and sequence ranges Author chain G; PDBConstruct 1–129; UniProt 42–170 Author chain I; PDBConstruct 1–129; UniProt 42–170 Author chain H; PDBConstruct 1–129; UniProt 42–170

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 5nbq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5nbq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5nbq
Deposition date deposition_date2017-03-02
Structure title titleThe structure of the tripartite complex between OspE, the C-terminal domains of factor H and C3dg
Keywords keywordscomplement, regulation, microbe, evasion, 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_guinier38.25
Radius of gyration Rg (electron density) rg_electron37.70
Forward intensity I(0) i0411215000.00
Molecular weight molecular_weight166860.0 kDa
Excluded volume excluded_volume209700 ų
Envelope volume envelope_volume277310 ų
Hydration-shell volume shell_volume60795 ų
Envelope diameter envelope_diameter147.1
Shell Rg shell_rg44.08
Envelope Rg envelope_rg37.48
Shape Rg shape_rg37.70
Total Rg total_rg38.13
Total atoms total_atoms11752
Residues n_residues1504
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 dmax137.7
Rg (real space) rg_real38.20
Rg uncertainty (real space) rg_real_error1.36
I(0) (real space) i0_real4.1120e+08
I(0) uncertainty (real space) i0_real_error7.2530e+06
Rg (reciprocal space) rg_reciprocal38.23
I(0) (reciprocal space) i0_reciprocal411200000.0000
Solution quality estimate total_estimate0.8479
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.0
Skewness Skewness skewness0.368
Kurtosis Kurtosis kurtosis-0.066
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha61400000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.691; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.948

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd5nbqa_
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_idd5nbqb_
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_idd5nbqc_
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 (11 domains)

Domain ID domain_id5nbqA00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id5nbqB00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id5nbqC00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id5nbqD01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id5nbqD02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id5nbqE01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id5nbqE02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id5nbqF01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id5nbqF02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id5nbqG00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology31 — Transcriptional Co-activator pc4; Chain A
Homologous superfamily homologous superfamily50 — Borrelia outer surface protein E/F
Domain ID domain_id5nbqI00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology31 — Transcriptional Co-activator pc4; Chain A
Homologous superfamily homologous superfamily50 — Borrelia outer surface protein E/F

8. Citations (1)

9. Files and Curves (10)