1ghq

CR2-C3D COMPLEX STRUCTURE

Method: X-RAY DIFFRACTION Dmax: 99.3 Å Quality: GOOD

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

COMPLEMENT C3

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 996–1300 Fragment:FRAGMENT OF ALPHA CHAIN Mutation:C17A CR2/CD121/C3D/EPSTEIN-BARR VIRUS RECEPTOR × 2 (P20023) ZN ZINC ION × 2 NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.04 Å R-free 0.239

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 3–308; UniProt 996–1300

CR2/CD121/C3D/EPSTEIN-BARR VIRUS RECEPTOR

OrganismNot specified

UniProt P20023

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 21–153 Chain C; UniProt 21–153 Fragment:SEQUENCE DATABASE RESIDUES 21-153 COMPLEMENT C3 × 1 (P01024) ZN ZINC ION × 2 NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.04 Å R-free 0.239

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.

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

View Construct and Data Evidence
UniProt name CR2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–134; UniProt 21–153 Author chain C; PDBConstruct 2–134; UniProt 21–153

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 1ghq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ghq
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1ghq
Deposition date deposition_date2001-01-11
Structure title titleCR2-C3D COMPLEX STRUCTURE
Keywords keywordsCR2, C3D, Immune system-viral protein receptor COMPLEX; Immune system/viral protein receptor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.60
Radius of gyration Rg (electron density) rg_electron30.30
Forward intensity I(0) i064472400.00
Molecular weight molecular_weight63643.0 kDa
Excluded volume excluded_volume79906 ų
Envelope volume envelope_volume104030 ų
Hydration-shell volume shell_volume30337 ų
Envelope diameter envelope_diameter105.7
Shell Rg shell_rg35.44
Envelope Rg envelope_rg30.15
Shape Rg shape_rg30.34
Total Rg total_rg30.67
Total atoms total_atoms4466
Residues n_residues570
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 dmax99.3
Rg (real space) rg_real30.77
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real6.4470e+07
I(0) uncertainty (real space) i0_real_error9.0270e+05
Rg (reciprocal space) rg_reciprocal30.70
I(0) (reciprocal space) i0_reciprocal64470000.0000
Solution quality estimate total_estimate0.8724
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.6
Skewness Skewness skewness0.442
Kurtosis Kurtosis kurtosis-0.447
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5714000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.882; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.903; Smooth: 0.788

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 13 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd1ghqa1
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_idd1ghqa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1ghqb1
Class classg — Small proteins
Fold Fold foldg.18 — Complement control module/SCR domain
Superfamily Superfamily superfamilyg.18.1 — Complement control module/SCR domain
Family Family familyg.18.1.1 — Complement control module/SCR domain
Domain ID domain_idd1ghqb2
Class classg — Small proteins
Fold Fold foldg.18 — Complement control module/SCR domain
Superfamily Superfamily superfamilyg.18.1 — Complement control module/SCR domain
Family Family familyg.18.1.1 — Complement control module/SCR domain
Domain ID domain_idd1ghqb3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1ghqc1
Class classg — Small proteins
Fold Fold foldg.18 — Complement control module/SCR domain
Superfamily Superfamily superfamilyg.18.1 — Complement control module/SCR domain
Family Family familyg.18.1.1 — Complement control module/SCR domain
Domain ID domain_idd1ghqc2
Class classg — Small proteins
Fold Fold foldg.18 — Complement control module/SCR domain
Superfamily Superfamily superfamilyg.18.1 — Complement control module/SCR domain
Family Family familyg.18.1.1 — Complement control module/SCR domain
Domain ID domain_idd1ghqc3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (5 domains)

Domain ID domain_id1ghqA00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id1ghqB01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id1ghqB02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id1ghqC01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id1ghqC02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1

8. Citations (1)

9. Files and Curves (10)