2ice

CRIg bound to C3c

Method: X-RAY DIFFRACTION Dmax: 172.7 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 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 23–664 Chain B; UniProt 749–954 Chain C; UniProt 1321–1663 Not recorded V-set and immunoglobulin domain-containing protein 4 × 1 (Q9Y279) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.10 Å R-free 0.295
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 23–664 Chain E; UniProt 749–954 Chain F; UniProt 1321–1663 Not recorded V-set and immunoglobulin domain-containing protein 4 × 1 (Q9Y279) CA CALCIUM ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.10 Å R-free 0.295

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, 2, 3
Chains and sequence ranges Author chain A; PDBConstruct 1–642; UniProt 23–664 Author chain D; PDBConstruct 1–642; UniProt 23–664 Author chain B; PDBConstruct 1–206; UniProt 749–954 Author chain E; PDBConstruct 1–206; UniProt 749–954 Author chain C; PDBConstruct 1–343; UniProt 1321–1663 Author chain F; PDBConstruct 1–343; UniProt 1321–1663

V-set and immunoglobulin domain-containing protein 4

Homo sapiens

UniProt Q9Y279

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 S; UniProt 19–137 Not recorded Complement C3 beta chain × 1 (P01024) Complement C3 alpha chain × 1 (P01024) Complement C3 alpha chain × 1 (P01024) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.10 Å R-free 0.295
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain T; UniProt 19–137 Not recorded Complement C3 beta chain × 1 (P01024) Complement C3 alpha chain × 1 (P01024) Complement C3 alpha chain × 1 (P01024) CA CALCIUM ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.10 Å R-free 0.295

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.

11 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VSIG4_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain S; PDBConstruct 1–119; UniProt 19–137 Author chain T; PDBConstruct 1–119; UniProt 19–137

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 2ice

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2ice
Deposition date deposition_date2006-09-12
Structure title titleCRIg bound to C3c
Keywords keywordsAlternative Pathway, Complement, C3, CRIg, Complement Receptor, 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_guinier51.15
Radius of gyration Rg (electron density) rg_electron50.58
Forward intensity I(0) i01094350000.00
Molecular weight molecular_weight278850.0 kDa
Excluded volume excluded_volume350570 ų
Envelope volume envelope_volume516260 ų
Hydration-shell volume shell_volume84624 ų
Envelope diameter envelope_diameter178.6
Shell Rg shell_rg54.31
Envelope Rg envelope_rg49.79
Shape Rg shape_rg50.57
Total Rg total_rg50.75
Total atoms total_atoms19619
Residues n_residues2468
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 dmax172.7
Rg (real space) rg_real51.10
Rg uncertainty (real space) rg_real_error1.77
I(0) (real space) i0_real1.0940e+09
I(0) uncertainty (real space) i0_real_error2.3350e+07
Rg (reciprocal space) rg_reciprocal51.17
I(0) (reciprocal space) i0_reciprocal1094000000.0000
Solution quality estimate total_estimate0.8878
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.3
Skewness Skewness skewness0.254
Kurtosis Kurtosis kurtosis-0.482
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha107800000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.874

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 22 domains

CATH v4.4 (22 domains)

Domain ID domain_id2iceA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1930 — Macroglobulin (MG2) domain
Domain ID domain_id2iceA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1930 — Macroglobulin (MG2) domain
Domain ID domain_id2iceA03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1940
Domain ID domain_id2iceA04
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2iceA05
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1930 — Macroglobulin (MG2) domain
Domain ID domain_id2iceA06
Class class6 — Special
Architecture architecture20 — Other non-globular
Topology topology50 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily160
Domain ID domain_id2iceB01
Class class2 — Mainly Beta
Architecture architecture20 — Single Sheet
Topology topology130 — S-adenosyl-L-methionine-dependent methyltransferases
Homologous superfamily homologous superfamily20
Domain ID domain_id2iceB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2iceC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily690 — Alpha-macroglobulin, receptor-binding domain
Domain ID domain_id2iceC02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily120
Domain ID domain_id2iceD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1930 — Macroglobulin (MG2) domain
Domain ID domain_id2iceD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1930 — Macroglobulin (MG2) domain
Domain ID domain_id2iceD03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1940
Domain ID domain_id2iceD04
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2iceD05
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1930 — Macroglobulin (MG2) domain
Domain ID domain_id2iceD06
Class class6 — Special
Architecture architecture20 — Other non-globular
Topology topology50 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily160
Domain ID domain_id2iceE01
Class class2 — Mainly Beta
Architecture architecture20 — Single Sheet
Topology topology130 — S-adenosyl-L-methionine-dependent methyltransferases
Homologous superfamily homologous superfamily20
Domain ID domain_id2iceE02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2iceF01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily690 — Alpha-macroglobulin, receptor-binding domain
Domain ID domain_id2iceF02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily120
Domain ID domain_id2iceS00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2iceT00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)