2wy7

Staphylococcus aureus complement subversion protein Sbi-IV in complex with complement fragment C3d revealing an alternative binding mode

Method: X-RAY DIFFRACTION Dmax: 72.3 Å Quality: GOOD

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

COMPLEMENT C3D FRAGMENT

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 996–1303 Fragment:C3D, RESIDUES 996-1303 Mutation:YES IGG-BINDING PROTEIN × 1 (C8LN82) GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;100MM TRIS PH8.0, 200MM NACL, 20%(W/V) PEG 4000 Resolution 1.70 Å R-free 0.205

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 117 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 3–310; UniProt 996–1303

IGG-BINDING PROTEIN

STAPHYLOCOCCUS AUREUS

UniProt C8LN82

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain Q; UniProt 198–266 Fragment:SBI-IV, RESIDUES 198-266 COMPLEMENT C3D FRAGMENT × 1 (P01024) GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;100MM TRIS PH8.0, 200MM NACL, 20%(W/V) PEG 4000 Resolution 1.70 Å R-free 0.205

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C8LN82_STAAU
Isoform
PDB entities 2
Chains and sequence ranges Author chain Q; PDBConstruct 12–80; UniProt 198–266

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 2wy7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2wy7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2wy7
Deposition date deposition_date2009-11-13
Structure title titleStaphylococcus aureus complement subversion protein Sbi-IV in complex with complement fragment C3d revealing an alternative binding mode
Keywords keywordsIMMUNE SYSTEM, IMMUNE RESPONSE, INNATE IMMUNITY, COMPLEMENT PATHWAY, INFLAMMATORY RESPONSE; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.76
Radius of gyration Rg (electron density) rg_electron20.60
Forward intensity I(0) i026702600.00
Molecular weight molecular_weight40298.0 kDa
Excluded volume excluded_volume50835 ų
Envelope volume envelope_volume58421 ų
Hydration-shell volume shell_volume23469 ų
Envelope diameter envelope_diameter74.3
Shell Rg shell_rg27.67
Envelope Rg envelope_rg21.00
Shape Rg shape_rg20.57
Total Rg total_rg21.60
Total atoms total_atoms2838
Residues n_residues357
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 dmax72.3
Rg (real space) rg_real21.66
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real2.6700e+07
I(0) uncertainty (real space) i0_real_error3.4140e+05
Rg (reciprocal space) rg_reciprocal21.68
I(0) (reciprocal space) i0_reciprocal26700000.0000
Solution quality estimate total_estimate0.8770
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.0
Skewness Skewness skewness0.257
Kurtosis Kurtosis kurtosis-0.288
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9985000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.930

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2wy7a_
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 (2 domains)

Domain ID domain_id2wy7A00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id2wy7Q00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily1270 — Sbi, C3 binding domain IV

8. Citations (1)

9. Files and Curves (10)