1bdc

STAPHYLOCOCCUS AUREUS PROTEIN A, IMMUNOGLOBULIN-BINDING B DOMAIN, NMR, 10 STRUCTURES

Method: SOLUTION NMR Dmax: 31.8 Å Quality: REASONABLE

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

STAPHYLOCOCCUS AUREUS PROTEIN A

Staphylococcus aureus

UniProt P38507

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 212–270 Fragment:B DOMAIN No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5;303 K Resolution not provided

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.

66 other PDB entries and 127 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPA2_STAAU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–60; UniProt 212–270

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 1bdc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bdc
Deposition date deposition_date1996-06-28
Structure title titleSTAPHYLOCOCCUS AUREUS PROTEIN A, IMMUNOGLOBULIN-BINDING B DOMAIN, NMR, 10 STRUCTURES
Keywords keywordsIMMUNOGLOBULIN-BINDING PROTEIN, TRANSMEMBRANE, CELL WALL, IMMUNOGLOBULIN BINDING DOMAIN; IMMUNOGLOBULIN-BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.35
Radius of gyration Rg (electron density) rg_electron11.94
Forward intensity I(0) i073011000.00
Molecular weight molecular_weight67684.0 kDa
Excluded volume excluded_volume83440 ų
Envelope volume envelope_volume16580 ų
Hydration-shell volume shell_volume10326 ų
Envelope diameter envelope_diameter55.2
Shell Rg shell_rg19.57
Envelope Rg envelope_rg15.30
Shape Rg shape_rg11.90
Total Rg total_rg12.39
Total atoms total_atoms9410
Residues n_residues600
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 dmax31.8
Rg (real space) rg_real11.62
Rg uncertainty (real space) rg_real_error0.04
I(0) (real space) i0_real6.9750e+07
I(0) uncertainty (real space) i0_real_error4.5480e+05
Rg (reciprocal space) rg_reciprocal12.44
I(0) (reciprocal space) i0_reciprocal73010000.0000
Solution quality estimate total_estimate0.6841
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary14.9
Skewness Skewness skewness0.189
Kurtosis Kurtosis kurtosis-0.383
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha3.1340
Highest regularization parameter α highest_alpha49820.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.981; Stabil: 0.984; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bdca_
Class classa — All alpha proteins
Fold Fold folda.8 — immunoglobulin/albumin-binding domain-like
Superfamily Superfamily superfamilya.8.1 — Bacterial immunoglobulin/albumin-binding domains
Family Family familya.8.1.1 — Immunoglobulin-binding protein A modules

CATH v4.4 (1 domains)

Domain ID domain_id1bdcA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily420 — Immunoglobulin FC, subunit C

8. Citations (4)

9. Files and Curves (10)