5fo7

Crystal Structure of Human Complement C3b at 2.8 Angstrom resolution

Method: X-RAY DIFFRACTION Dmax: 160.7 Å Quality: GOOD

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

COMPLEMENT C3 BETA CHAIN

OrganismNot specified

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 23–667 Chain B; UniProt 749–1663 Fragment:RESIDUES 23-667 Fragment:RESIDUES 749-1663 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:8% PEG 3350 35MM BIS-TRIS PH 5.5 Resolution 2.80 Å R-free 0.268

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, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–645; UniProt 23–667 Author chain B; PDBConstruct 1–915; UniProt 749–1663

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 5fo7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5fo7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5fo7
Deposition date deposition_date2015-11-18
Structure title titleCrystal Structure of Human Complement C3b at 2.8 Angstrom resolution
Keywords keywordsLIPID BINDING, COMPLEMENT SYSTEM, IMMUNE SYSTEM, PLASMA PROTEIN; LIPID BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier46.29
Radius of gyration Rg (electron density) rg_electron46.16
Forward intensity I(0) i0432060000.00
Molecular weight molecular_weight172650.0 kDa
Excluded volume excluded_volume217050 ų
Envelope volume envelope_volume313610 ų
Hydration-shell volume shell_volume59571 ų
Envelope diameter envelope_diameter171.0
Shell Rg shell_rg47.51
Envelope Rg envelope_rg45.23
Shape Rg shape_rg46.15
Total Rg total_rg46.24
Total atoms total_atoms12150
Residues n_residues1537
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 dmax160.7
Rg (real space) rg_real46.54
Rg uncertainty (real space) rg_real_error1.69
I(0) (real space) i0_real4.3210e+08
I(0) uncertainty (real space) i0_real_error8.6200e+06
Rg (reciprocal space) rg_reciprocal46.29
I(0) (reciprocal space) i0_reciprocal431900000.0000
Solution quality estimate total_estimate0.8673
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.0
Skewness Skewness skewness0.438
Kurtosis Kurtosis kurtosis-0.338
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha29680000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.831; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.805

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id5fo7A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1930 — Macroglobulin (MG2) domain
Domain ID domain_id5fo7A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1930 — Macroglobulin (MG2) domain
Domain ID domain_id5fo7A03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1940
Domain ID domain_id5fo7A04
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5fo7A05
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1930 — Macroglobulin (MG2) domain
Domain ID domain_id5fo7A06
Class class6 — Special
Architecture architecture20 — Other non-globular
Topology topology50 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily160
Domain ID domain_id5fo7B01
Class class2 — Mainly Beta
Architecture architecture20 — Single Sheet
Topology topology130 — S-adenosyl-L-methionine-dependent methyltransferases
Homologous superfamily homologous superfamily20
Domain ID domain_id5fo7B02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5fo7B03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily1540
Domain ID domain_id5fo7B04
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id5fo7B05
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily690 — Alpha-macroglobulin, receptor-binding domain
Domain ID domain_id5fo7B06
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily120

8. Citations (1)

9. Files and Curves (10)