3hrz

Cobra Venom Factor (CVF) in complex with human factor B

Method: X-RAY DIFFRACTION Dmax: 144.9 Å Quality: GOOD

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

Cobra venom factor

OrganismNot specified

UniProt Q91132

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 23–649 Chain B; UniProt 733–984 Chain C; UniProt 1264–1642 Fragment:residues 23-649 Fragment:residues 733-984 Fragment:residues 1264-1642 Complement factor B × 1 (P00751) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 MG MAGNESIUM ION × 2 K POTASSIUM ION × 1 P6G HEXAETHYLENE GLYCOL × 2 PO4 PHOSPHATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;PEG 3350, PEG 400, Na/K Phosphate, Bis-Tris propane, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.20 Å R-free 0.226

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.

5 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CO3_NAJKA
Isoform
PDB entities 1, 2, 3
Chains and sequence ranges Author chain A; PDBConstruct 1–627; UniProt 23–649 Author chain B; PDBConstruct 1–252; UniProt 733–984 Author chain C; PDBConstruct 1–379; UniProt 1264–1642

Complement factor B

Homo sapiens

UniProt P00751

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 26–764 Fragment:residues 26-764 Mutation:D279G,N285D Cobra venom factor × 1 (Q91132) Cobra venom factor × 1 (Q91132) Cobra venom factor × 1 (Q91132) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 MG MAGNESIUM ION × 2 K POTASSIUM ION × 1 P6G HEXAETHYLENE GLYCOL × 2 PO4 PHOSPHATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;PEG 3350, PEG 400, Na/K Phosphate, Bis-Tris propane, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.20 Å R-free 0.226

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.

25 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CFAB_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–739; UniProt 26–764

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 3hrz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3hrz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3hrz
Deposition date deposition_date2009-06-10
Structure title titleCobra Venom Factor (CVF) in complex with human factor B
Keywords keywords;serine protease, glycosilated, multi-domain, complement system, convertase, Complement alternate pathway, Complement pathway, Disulfide bond, Glycoprotein, Immune response, Inflammatory response, Innate immunity, Secreted, Thioester bond, Cleavage on pair of basic residues, Glycation, Hydrolase, Protease, Sushi, Zymogen, IMMUNE SYSTEM ;; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.29
Radius of gyration Rg (electron density) rg_electron43.97
Forward intensity I(0) i0680161000.00
Molecular weight molecular_weight215990.0 kDa
Excluded volume excluded_volume270840 ų
Envelope volume envelope_volume371020 ų
Hydration-shell volume shell_volume70956 ų
Envelope diameter envelope_diameter155.1
Shell Rg shell_rg48.48
Envelope Rg envelope_rg43.20
Shape Rg shape_rg43.97
Total Rg total_rg44.17
Total atoms total_atoms15187
Residues n_residues1902
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 dmax144.9
Rg (real space) rg_real44.26
Rg uncertainty (real space) rg_real_error1.14
I(0) (real space) i0_real6.8020e+08
I(0) uncertainty (real space) i0_real_error1.3150e+07
Rg (reciprocal space) rg_reciprocal44.29
I(0) (reciprocal space) i0_reciprocal680200000.0000
Solution quality estimate total_estimate0.8936
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.3
Skewness Skewness skewness0.284
Kurtosis Kurtosis kurtosis-0.482
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha75110000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.871

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 11 domains

CATH v4.4 (11 domains)

Domain ID domain_id3hrzA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1930 — Macroglobulin (MG2) domain
Domain ID domain_id3hrzA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1930 — Macroglobulin (MG2) domain
Domain ID domain_id3hrzA03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1940
Domain ID domain_id3hrzA04
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3hrzA05
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1930 — Macroglobulin (MG2) domain
Domain ID domain_id3hrzA06
Class class6 — Special
Architecture architecture20 — Other non-globular
Topology topology50 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily160
Domain ID domain_id3hrzB01
Class class2 — Mainly Beta
Architecture architecture20 — Single Sheet
Topology topology130 — S-adenosyl-L-methionine-dependent methyltransferases
Homologous superfamily homologous superfamily20
Domain ID domain_id3hrzB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3hrzC01
Class class2 — Mainly Beta
Architecture architecture20 — Single Sheet
Topology topology210 — ubp-family deubiquitinating enzyme fold
Homologous superfamily homologous superfamily20
Domain ID domain_id3hrzC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily690 — Alpha-macroglobulin, receptor-binding domain
Domain ID domain_id3hrzC03
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)