2gox

Crystal structure of Efb-C / C3d Complex

Method: X-RAY DIFFRACTION Dmax: 93.6 Å Quality: REASONABLE

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 996–1287 Fragment:Fragment of alpha chain: Residues 996-1287 Mutation:C1010A Fibrinogen-binding protein × 1 (P68799) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;60% Tacsimate pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 2.20 Å R-free 0.231
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 996–1287 Fragment:Fragment of alpha chain: Residues 996-1287 Mutation:C1010A Fibrinogen-binding protein × 1 (P68799) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;60% Tacsimate pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 2.20 Å R-free 0.231

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 116 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 6–297; UniProt 996–1287 Author chain C; PDBConstruct 6–297; UniProt 996–1287

Fibrinogen-binding protein

Staphylococcus aureus subsp. aureus Mu50

UniProt P68799

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 B; UniProt 101–165 Fragment:C-terminal domain: Residues 101-165 Complement C3 × 1 (P01024) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;60% Tacsimate pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 2.20 Å R-free 0.231
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 101–165 Fragment:C-terminal domain: Residues 101-165 Complement C3 × 1 (P01024) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;60% Tacsimate pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 2.20 Å R-free 0.231

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 FIB_STAAM
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–65; UniProt 101–165 Author chain D; PDBConstruct 1–65; UniProt 101–165

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 2gox

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2gox
Deposition date deposition_date2006-04-14
Structure title titleCrystal structure of Efb-C / C3d Complex
Keywords keywordsPROTEIN-PROTEIN COMPLEX, CELL ADHESION-TOXIN COMPLEX; CELL ADHESION/TOXIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.81
Radius of gyration Rg (electron density) rg_electron27.98
Forward intensity I(0) i099913800.00
Molecular weight molecular_weight80502.0 kDa
Excluded volume excluded_volume101700 ų
Envelope volume envelope_volume120880 ų
Hydration-shell volume shell_volume35753 ų
Envelope diameter envelope_diameter100.1
Shell Rg shell_rg35.39
Envelope Rg envelope_rg28.07
Shape Rg shape_rg27.93
Total Rg total_rg28.87
Total atoms total_atoms5674
Residues n_residues724
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 dmax93.6
Rg (real space) rg_real28.76
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real9.9910e+07
I(0) uncertainty (real space) i0_real_error1.2670e+06
Rg (reciprocal space) rg_reciprocal28.79
I(0) (reciprocal space) i0_reciprocal99920000.0000
Solution quality estimate total_estimate0.6804
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.0
Skewness Skewness skewness0.290
Kurtosis Kurtosis kurtosis-0.451
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21870000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.992; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd2goxa1
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_idd2goxa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2goxb1
Class classa — All alpha proteins
Fold Fold folda.7 — Spectrin repeat-like
Superfamily Superfamily superfamilya.7.17 — Efb C-domain-like
Family Family familya.7.17.1 — Efb C-domain-like
Domain ID domain_idd2goxc1
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_idd2goxc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2goxd_
Class classa — All alpha proteins
Fold Fold folda.7 — Spectrin repeat-like
Superfamily Superfamily superfamilya.7.17 — Efb C-domain-like
Family Family familya.7.17.1 — Efb C-domain-like

CATH v4.4 (4 domains)

Domain ID domain_id2goxA00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id2goxB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily1270 — Sbi, C3 binding domain IV
Domain ID domain_id2goxC00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id2goxD00
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)