1fcc

CRYSTAL STRUCTURE OF THE C2 FRAGMENT OF STREPTOCOCCAL PROTEIN G IN COMPLEX WITH THE FC DOMAIN OF HUMAN IGG

Method: X-RAY DIFFRACTION Dmax: 91.7 Å Quality: EXCELLENT

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

IGG1 MO61 FC

Homo sapiens

UniProt P01857

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 121–326 Chain B; UniProt 121–326 Not recorded STREPTOCOCCAL PROTEIN G (C2 FRAGMENT) × 2 (P19909) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.20 Å R-free 0.357

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.

134 other PDB entries and 162 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGHG1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–206; UniProt 121–326 Author chain B; PDBConstruct 1–206; UniProt 121–326

STREPTOCOCCAL PROTEIN G (C2 FRAGMENT)

Streptococcus

UniProt P19909

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 372–427 Chain D; UniProt 372–427 Not recorded IGG1 MO61 FC × 2 (P01857) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.20 Å R-free 0.357

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.

76 other PDB entries and 116 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPG2_STRSG
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–56; UniProt 372–427 Author chain D; PDBConstruct 1–56; UniProt 372–427

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 1fcc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1fcc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1fcc
Deposition date deposition_date1995-01-17
Structure title titleCRYSTAL STRUCTURE OF THE C2 FRAGMENT OF STREPTOCOCCAL PROTEIN G IN COMPLEX WITH THE FC DOMAIN OF HUMAN IGG
Keywords keywordsCOMPLEX (ANTIBODY-ANTIGEN), COMPLEX (ANTIBODY-ANTIGEN) complex; COMPLEX (ANTIBODY/ANTIGEN)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.58
Radius of gyration Rg (electron density) rg_electron28.57
Forward intensity I(0) i057322400.00
Molecular weight molecular_weight59281.0 kDa
Excluded volume excluded_volume74235 ų
Envelope volume envelope_volume100190 ų
Hydration-shell volume shell_volume29471 ų
Envelope diameter envelope_diameter89.5
Shell Rg shell_rg35.65
Envelope Rg envelope_rg28.14
Shape Rg shape_rg28.55
Total Rg total_rg29.36
Total atoms total_atoms4180
Residues n_residues524
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 dmax91.7
Rg (real space) rg_real29.49
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real5.7320e+07
I(0) uncertainty (real space) i0_real_error8.3070e+05
Rg (reciprocal space) rg_reciprocal29.53
I(0) (reciprocal space) i0_reciprocal57320000.0000
Solution quality estimate total_estimate0.9134
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.8
Skewness Skewness skewness0.119
Kurtosis Kurtosis kurtosis-0.656
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha8167000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.968; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.970

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1fcca1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd1fcca2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd1fccb1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd1fccb2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd1fccc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.7 — Immunoglobulin-binding domains
Family Family familyd.15.7.1 — Immunoglobulin-binding domains
Domain ID domain_idd1fccd_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.7 — Immunoglobulin-binding domains
Family Family familyd.15.7.1 — Immunoglobulin-binding domains

CATH v4.4 (6 domains)

Domain ID domain_id1fccA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1fccA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1fccB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1fccB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1fccC00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily10
Domain ID domain_id1fccD00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)