1igd

THE THIRD IGG-BINDING DOMAIN FROM STREPTOCOCCAL PROTEIN G: AN ANALYSIS BY X-RAY CRYSTALLOGRAPHY OF THE STRUCTURE ALONE AND IN A COMPLEX WITH FAB

Method: X-RAY DIFFRACTION Dmax: 51.0 Å Quality: GOOD

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

PROTEIN G

Streptococcus sp. G148

UniProt P06654

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 293–352 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.10 Å

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.

48 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPG1_STRSG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–61; UniProt 293–352

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 1igd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1igd
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1igd
Deposition date deposition_date1994-08-05
Structure title titleTHE THIRD IGG-BINDING DOMAIN FROM STREPTOCOCCAL PROTEIN G: AN ANALYSIS BY X-RAY CRYSTALLOGRAPHY OF THE STRUCTURE ALONE AND IN A COMPLEX WITH FAB
Keywords keywordsIMMUNOGLOBULIN BINDING PROTEIN; IMMUNOGLOBULIN BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier12.96
Radius of gyration Rg (electron density) rg_electron11.79
Forward intensity I(0) i01026270.00
Molecular weight molecular_weight6648.0 kDa
Excluded volume excluded_volume8321 ų
Envelope volume envelope_volume9504 ų
Hydration-shell volume shell_volume7506 ų
Envelope diameter envelope_diameter48.3
Shell Rg shell_rg16.54
Envelope Rg envelope_rg12.51
Shape Rg shape_rg11.66
Total Rg total_rg13.40
Total atoms total_atoms468
Residues n_residues61
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 dmax51.0
Rg (real space) rg_real13.03
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real1.0260e+06
I(0) uncertainty (real space) i0_real_error1.1570e+04
Rg (reciprocal space) rg_reciprocal13.02
I(0) (reciprocal space) i0_reciprocal1026000.0000
Solution quality estimate total_estimate0.7609
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.8
Skewness Skewness skewness0.582
Kurtosis Kurtosis kurtosis0.470
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha207300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.397; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.712; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1igda_
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 (1 domains)

Domain ID domain_id1igdA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily10

8. Citations (6)

9. Files and Curves (10)