2xqw

Structure of Factor H domains 19-20 in complex with complement C3d

Method: X-RAY DIFFRACTION Dmax: 106.1 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 996–1287 Chain B; UniProt 996–1287 Fragment:THIOESTER DOMAIN, RESIDUES 996-1287 Mutation:YES COMPLEMENT FACTOR H × 1 (P08603) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;295 K;12-18% PEG 4000, 0.1 M HEPES, PH 7.5, AT 22 DEGREES C Resolution 2.31 Å R-free 0.242
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 996–1287 Fragment:THIOESTER DOMAIN, RESIDUES 996-1287 Mutation:YES No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;295 K;12-18% PEG 4000, 0.1 M HEPES, PH 7.5, AT 22 DEGREES C Resolution 2.31 Å R-free 0.242
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 996–1287 Fragment:THIOESTER DOMAIN, RESIDUES 996-1287 Mutation:YES No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;295 K;12-18% PEG 4000, 0.1 M HEPES, PH 7.5, AT 22 DEGREES C Resolution 2.31 Å R-free 0.242

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 3–294; UniProt 996–1287 Author chain B; PDBConstruct 3–294; UniProt 996–1287

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 C; UniProt 1103–1231 Fragment:DOMAINS 19-20, RESIDUES 1103-1231 Mutation:YES COMPLEMENT C3 × 2 (P01024) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;295 K;12-18% PEG 4000, 0.1 M HEPES, PH 7.5, AT 22 DEGREES C Resolution 2.31 Å R-free 0.242
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1103–1231 Fragment:DOMAINS 19-20, RESIDUES 1103-1231 Mutation:YES No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;295 K;12-18% PEG 4000, 0.1 M HEPES, PH 7.5, AT 22 DEGREES C Resolution 2.31 Å R-free 0.242

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 74 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 C; PDBConstruct 5–133; UniProt 1103–1231

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 2xqw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2xqw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2xqw
Deposition date deposition_date2010-09-07
Structure title titleStructure of Factor H domains 19-20 in complex with complement C3d
Keywords keywordsIMMUNE SYSTEM, COMPLEMENT ALTERNATIVE PATHWAY, ATYPICAL HEMOLYTIC UREMIC SYNDROME, AHUS, CFH, FH, C3B; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.29
Radius of gyration Rg (electron density) rg_electron31.86
Forward intensity I(0) i092351200.00
Molecular weight molecular_weight78169.0 kDa
Excluded volume excluded_volume98535 ų
Envelope volume envelope_volume120270 ų
Hydration-shell volume shell_volume32313 ų
Envelope diameter envelope_diameter109.4
Shell Rg shell_rg37.57
Envelope Rg envelope_rg31.59
Shape Rg shape_rg31.87
Total Rg total_rg32.33
Total atoms total_atoms5507
Residues n_residues711
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 dmax106.1
Rg (real space) rg_real32.44
Rg uncertainty (real space) rg_real_error0.98
I(0) (real space) i0_real9.2350e+07
I(0) uncertainty (real space) i0_real_error1.3670e+06
Rg (reciprocal space) rg_reciprocal32.38
I(0) (reciprocal space) i0_reciprocal92350000.0000
Solution quality estimate total_estimate0.8706
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.3
Skewness Skewness skewness0.370
Kurtosis Kurtosis kurtosis-0.606
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16940000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.899; Smooth: 0.842

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2xqwa1
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_idd2xqwa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2xqwb1
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_idd2xqwb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (4 domains)

Domain ID domain_id2xqwA00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id2xqwB00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id2xqwC01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id2xqwC02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1

8. Citations (3)

9. Files and Curves (10)