SAXSdb — 2w81

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

COMPLEMENT FACTOR H

HOMO SAPIENS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	FACTOR H BINDING PROTEIN × 1 （Q9JXV4） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	FACTOR H BINDING PROTEIN × 1 （Q9JXV4） water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	FACTOR H BINDING PROTEIN × 1 （Q9JXV4） water × 2	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	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–123； UniProt 321–443 Author chain B； PDBConstruct 1–123； UniProt 321–443 Author chain E； PDBConstruct 1–123； UniProt 321–443

FACTOR H BINDING PROTEIN

NEISSERIA MENINGITIDIS

UniProt Q9JXV4

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	COMPLEMENT FACTOR H × 1 （P08603） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	COMPLEMENT FACTOR H × 1 （P08603） water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	COMPLEMENT FACTOR H × 1 （P08603） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9JXV4_NEIMB
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–250； UniProt 71–320 Author chain D； PDBConstruct 1–250； UniProt 71–320 Author chain F； PDBConstruct 1–250； UniProt 71–320

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	2w81
Deposition date deposition_date	2009-01-08
Structure title title	Structure of a complex between Neisseria meningitidis factor H binding protein and CCPs 6-7 of human complement factor H
Keywords keywords	;GLYCOPROTEIN, IMMUNE EVASION, AGE-RELATED MACULAR DEGENERATION, INNATE IMMUNITY, IMMUNE RESPONSE, DISEASE MUTATION, FACTOR H, COMPLEMENT ALTERNATE PATHWAY, VACCINE CANDIDATE, 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.

2w81__assembly_1__model_1

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

Download this curve (.dat)

2w81__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2w81__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	23.14 Å
Rg (electron density)	22.45 Å
Total Rg	23.30 Å
Atom count	2788
Residues	358
Excluded volume	49009 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2w81__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2w81__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2w81__assembly_3__model_1`	dimeric （2）	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	COMPLEMENT FACTOR H
Molecular weight formula_weight	14222.0 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,E
Atom count atom_count	8836

TLKPCDYPDIKHGGLYHENMRRPYFPVAVGKYYSYYCDEHFETPSGSYWDHIHCTQDGWSPAVPCLRKCYFPYLENGYNQNHGRKFVQGKSIDVACHPGYALPKAQTTVTCMENGWSPTPRCI

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

Entity 2 Entity 2 polymer

Description description	FACTOR H BINDING PROTEIN
Molecular weight formula_weight	26983.1 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

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

GGVAADIGAGLADALTAPLDHKDKGLQSLTLDQSVRKNEKLKLAAQGAEKTYGNGDSLNTGKLKNDKVSRFDFIRQIEVDGQLITLESGEFQVYKQSHSALTAFQTEQIQDSEHSGKMVAKRQFRIGDIAGEHTSFDKLPEGGRATYRGTAFGSDDAGGKLTYTIDFAAKQGNGKIEHLKSPELNVDLAAADIKPDGKRHAVISGSVLYNQAEKGSYSLGIFGGKAQEVAGSAEVKTVNGIRHIGLAAKQELE

Source Source

Source organism organism	NEISSERIA MENINGITIDIS
NCBI taxonomy ID ncbi_taxonomy_id	487
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	424

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6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id	2w81A01
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	2w81A02
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	2w81B01
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	2w81B02
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	2w81C01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1980 —

Domain ID domain_id	2w81C02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	160 — Porin
Homologous superfamily homologous superfamily	90 —

Domain ID domain_id	2w81D01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1980 —

Domain ID domain_id	2w81D02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	160 — Porin
Homologous superfamily homologous superfamily	90 —

Domain ID domain_id	2w81E01
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	2w81E02
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	2w81F01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1980 —

Domain ID domain_id	2w81F02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	160 — Porin
Homologous superfamily homologous superfamily	90 —

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Unit-cell length a length_a	185.520 Å
Unit-cell length b length_b	52.210 Å
Unit-cell length c length_c	128.780 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	118.19 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.350 Å
Low-resolution limit resolution_low	38.810 Å
R factor r_factor	0.2750
R_work r_work	0.2740
R_free r_free	0.2830

Structure of a complex between Neisseria meningitidis factor H binding protein and CCPs 6-7 of human complement factor H

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

COMPLEMENT FACTOR H

State in the Current Structure

Other States of the Same Protein in the Database

FACTOR H BINDING PROTEIN

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

2w81__assembly_1__model_1

2w81__assembly_1__model_1 | I(q)

2w81__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 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

7. Citations (1)

Structure of a complex between Neisseria meningitidis factor H binding protein and CCPs 6-7 of human complement factor H

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

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

FACTOR H BINDING PROTEIN

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

2w81__assembly_1__model_1

2w81__assembly_1__model_1 | I(q)

2w81__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 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

7. Citations (1)