5nbq

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

Method: X-RAY DIFFRACTION

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

Complement C3

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Complement factor H × 1 （P08603） Outer surface protein E × 1 （Q45001） water × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Complement factor H × 1 （P08603） Outer surface protein E,Outer surface protein E × 1 （Q45001）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	Complement factor H × 1 （P08603） Outer surface protein E × 1 （Q45001） water × 1	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Complement C3 × 1 （P01024） Outer surface protein E × 1 （Q45001） water × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Complement C3 × 1 （P01024） Outer surface protein E,Outer surface protein E × 1 （Q45001）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	Complement C3 × 1 （P01024） Outer surface protein E × 1 （Q45001） water × 1	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Complement C3 × 1 （P01024） Complement factor H × 1 （P08603） water × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Complement C3 × 1 （P01024） Complement factor H × 1 （P08603）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	Complement C3 × 1 （P01024） Complement factor H × 1 （P08603） water × 1	Consistent with protein count

Other States of the Same Protein in the Database

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	5nbq
Deposition date deposition_date	2017-03-02
Structure title title	The structure of the tripartite complex between OspE, the C-terminal domains of factor H and C3dg
Keywords keywords	complement, regulation, microbe, evasion, immune system; IMMUNE SYSTEM
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

5nbq__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5nbq__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5nbq__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	27.97 Å
Rg (electron density)	27.05 Å
Total Rg	27.75 Å
Atom count	4244
Residues	546
Excluded volume	75529 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5nbq__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`5nbq__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`5nbq__assembly_3__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Complement C3
Molecular weight formula_weight	32824.6 kDa
Mutation mutation	A1153E, C1010A
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	11754

AVDAERLKHLIVTPSGAGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAP

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Complement factor H
Molecular weight formula_weight	14443.4 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,E,F

DSTGKCGPPPPIDNGDITSFPLSVYAPASSVEYQCQNLYQLEGNKRITCRNGQWSEPPKCLHPCVISREIMENYNIALRWTAKQKLYSRTGESVEFVCKRGYRLSSRSHTLRTTCWDGKLEYPTCAK

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Pichia

Entity 3 Entity 3 polymer

Description description	Outer surface protein E
Molecular weight formula_weight	14385.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,I

SKFTVKIKNKDKSGNWTDLGDLVVRKEENGIDTGLNAGGHSATFFSLEEEVVNNFVKVMTEGGSFKTSLYYGYKEEQSVINGIQNKEIITKIEKIDGTEYITFSGDKIKNSGDKVAEYAISLEELKKNL

Source Source

Source organism organism	Borreliella burgdorferi
Common name common_name	Lyme disease spirochete
NCBI taxonomy ID ncbi_taxonomy_id	139
Host organism host_organism	Escherichia coli

Entity 4 Entity 4 polymer

Description description	Outer surface protein E,Outer surface protein E
Molecular weight formula_weight	14810.6 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

SKFTVKIKNKDKSGNWTDLGDLVVRKEENGIDTGLNAGGHSATFFSLEEEVVNNFVKVMTEGGSFKTSLYYGYKEEQSVINGIQNKEIITKIEKIDGTEYITFSGDKIKNSGDKVAEYAISLEELKKNLXXXXX

Source Source

Source organism organism	Borreliella burgdorferi
Common name common_name	Lyme disease spirochete
NCBI taxonomy ID ncbi_taxonomy_id	139
Host organism host_organism	Escherichia coli

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	2

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6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d5nbqa_
Class class	a — All alpha proteins
Fold Fold fold	a.102 — alpha/alpha toroid
Superfamily Superfamily superfamily	a.102.4 — Terpenoid cyclases/Protein prenyltransferases
Family Family family	a.102.4.4 — Complement components

Domain ID domain_id	d5nbqb_
Class class	a — All alpha proteins
Fold Fold fold	a.102 — alpha/alpha toroid
Superfamily Superfamily superfamily	a.102.4 — Terpenoid cyclases/Protein prenyltransferases
Family Family family	a.102.4.4 — Complement components

Domain ID domain_id	d5nbqc_
Class class	a — All alpha proteins
Fold Fold fold	a.102 — alpha/alpha toroid
Superfamily Superfamily superfamily	a.102.4 — Terpenoid cyclases/Protein prenyltransferases
Family Family family	a.102.4.4 — Complement components

CATH v4.4 (11 domains)

Domain ID domain_id	5nbqA00
Class class	1 — Mainly Alpha
Architecture architecture	50 — Alpha/alpha barrel
Topology topology	10 — Glycosyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	5nbqB00
Class class	1 — Mainly Alpha
Architecture architecture	50 — Alpha/alpha barrel
Topology topology	10 — Glycosyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	5nbqC00
Class class	1 — Mainly Alpha
Architecture architecture	50 — Alpha/alpha barrel
Topology topology	10 — Glycosyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	5nbqD01
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	70 — Complement Module; domain 1
Homologous superfamily homologous superfamily	10 — Complement Module, domain 1

Domain ID domain_id	5nbqD02
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	70 — Complement Module; domain 1
Homologous superfamily homologous superfamily	10 — Complement Module, domain 1

Domain ID domain_id	5nbqE01
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	70 — Complement Module; domain 1
Homologous superfamily homologous superfamily	10 — Complement Module, domain 1

Domain ID domain_id	5nbqE02
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	70 — Complement Module; domain 1
Homologous superfamily homologous superfamily	10 — Complement Module, domain 1

Domain ID domain_id	5nbqF01
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	70 — Complement Module; domain 1
Homologous superfamily homologous superfamily	10 — Complement Module, domain 1

Domain ID domain_id	5nbqF02
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	70 — Complement Module; domain 1
Homologous superfamily homologous superfamily	10 — Complement Module, domain 1

Domain ID domain_id	5nbqG00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	31 — Transcriptional Co-activator pc4; Chain A
Homologous superfamily homologous superfamily	50 — Borrelia outer surface protein E/F

Domain ID domain_id	5nbqI00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	31 — Transcriptional Co-activator pc4; Chain A
Homologous superfamily homologous superfamily	50 — Borrelia outer surface protein E/F

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Unit-cell length a length_a	124.907 Å
Unit-cell length b length_b	165.063 Å
Unit-cell length c length_c	84.185 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	3.180 Å
Low-resolution limit resolution_low	29.600 Å
R factor r_factor	0.2350
R_work r_work	0.2330
R_free r_free	0.2610

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

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

Complement C3

State in the Current Structure

Other States of the Same Protein in the Database

Complement factor H

State in the Current Structure

Other States of the Same Protein in the Database

Outer surface protein E

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

5nbq__assembly_1__model_1

5nbq__assembly_1__model_1 | I(q)

5nbq__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (3 domains)

CATH v4.4 (11 domains)

7. Citations (1)

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

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

Complement C3

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Complement factor H

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Outer surface protein E

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

5nbq__assembly_1__model_1

5nbq__assembly_1__model_1 | I(q)

5nbq__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (3 domains)

CATH v4.4 (11 domains)

7. Citations (1)