SAXSdb — 1ggq

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

OUTER SURFACE PROTEIN C

Borrelia burgdorferi

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	MAGNESIUM ION × 1 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 4	MAGNESIUM ION × 1 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	OSPC1_BORBU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–174； UniProt 38–210 Author chain B； PDBConstruct 2–174； UniProt 38–210 Author chain C； PDBConstruct 2–174； UniProt 38–210 Author chain D； PDBConstruct 2–174； UniProt 38–210

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	1ggq
Deposition date deposition_date	2000-09-14
Structure title title	OUTER SURFACE PROTEIN C (OSPC) OF BORRELIA BURGDORFERI STRAIN B31
Keywords keywords	Lyme disease antigen, helical bundle, homodimer, MEMBRANE PROTEIN; MEMBRANE PROTEIN
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.

1ggq__assembly_1__model_1

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

Download this curve (.dat)

1ggq__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1ggq__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.25 Å
Rg (electron density)	21.10 Å
Total Rg	21.96 Å
Atom count	2424
Residues	324
Excluded volume	43588 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1ggq__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1ggq__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1ggq__assembly_3__model_1`	tetrameric （4）	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 (3)

Entity 1 Entity 1 polymer

Description description	OUTER SURFACE PROTEIN C
Molecular weight formula_weight	18597.4 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	4959

MKGPNLTEISKKITDSNAVLLAVKEVEALLSSIDEIAAKAIGKKIHQNNGLDTENNHNGSLLAGAYAISTLIKQKLDGLKNEGLKEKIDAAKKCSETFTNKLKEKHTDLGKEGVTDADAKEAILKTNGTKTKGAEELGKLFESVEVLSKAAKEMLANSVKELTSPVVAESPKKP

Source Source

Source organism organism	Borrelia burgdorferi
NCBI taxonomy ID ncbi_taxonomy_id	224326
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	112

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1ggqa_
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.12 — Outer surface protein C (OspC)
Family Family family	a.24.12.1 — Outer surface protein C (OspC)

Domain ID domain_id	d1ggqb_
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.12 — Outer surface protein C (OspC)
Family Family family	a.24.12.1 — Outer surface protein C (OspC)

Domain ID domain_id	d1ggqc_
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.12 — Outer surface protein C (OspC)
Family Family family	a.24.12.1 — Outer surface protein C (OspC)

Domain ID domain_id	d1ggqd_
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.12 — Outer surface protein C (OspC)
Family Family family	a.24.12.1 — Outer surface protein C (OspC)

CATH v4.4 (4 domains)

Domain ID domain_id	1ggqA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	240 — Lipoprotein, type 6

Domain ID domain_id	1ggqB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	240 — Lipoprotein, type 6

Domain ID domain_id	1ggqC00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	240 — Lipoprotein, type 6

Domain ID domain_id	1ggqD00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	240 — Lipoprotein, type 6

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Unit-cell length a length_a	127.206 Å
Unit-cell length b length_b	33.654 Å
Unit-cell length c length_c	47.993 Å
Unit-cell angle α angle_alpha	84.04 °
Unit-cell angle β angle_beta	81.55 °
Unit-cell angle γ angle_gamma	89.23 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.510 Å
Low-resolution limit resolution_low	40.740 Å
R factor r_factor	0.2310
R_work r_work	0.2310
R_free r_free	0.2650

OUTER SURFACE PROTEIN C (OSPC) OF BORRELIA BURGDORFERI STRAIN B31

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

OUTER SURFACE PROTEIN C

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

1ggq__assembly_1__model_1

1ggq__assembly_1__model_1 | I(q)

1ggq__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

OUTER SURFACE PROTEIN C (OSPC) OF BORRELIA BURGDORFERI STRAIN B31

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

OUTER SURFACE PROTEIN C

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

1ggq__assembly_1__model_1

1ggq__assembly_1__model_1 | I(q)

1ggq__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)