2jwd

protein A

Method: SOLUTION NMR Dmax: 49.6 Å Quality: REASONABLE

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

Immunoglobulin G-binding 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 213–269 Fragment:B domain Mutation:Y15W No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5;298 K;Ionic strength (raw mmCIF value) 100;Pressure ambient NMR sample composition:20mM sodium acetate, 100mM sodium chloride, 90% H2O/10% D2O | 90% H2O/10% D2O 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 3–59; UniProt 213–269

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 2jwd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2jwd
Deposition date deposition_date2007-10-09
Structure title titleprotein A
Keywords keywordsprotein a, poly glutamine, Cell wall, IgG-binding protein, Peptidoglycan-anchor, Secreted, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.76
Radius of gyration Rg (electron density) rg_electron12.63
Forward intensity I(0) i0584636000.00
Molecular weight molecular_weight196080.0 kDa
Excluded volume excluded_volume241740 ų
Envelope volume envelope_volume21744 ų
Hydration-shell volume shell_volume12040 ų
Envelope diameter envelope_diameter56.9
Shell Rg shell_rg21.17
Envelope Rg envelope_rg17.04
Shape Rg shape_rg12.59
Total Rg total_rg12.91
Total atoms total_atoms27231
Residues n_residues1711
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 dmax49.6
Rg (real space) rg_real12.86
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real5.8460e+08
I(0) uncertainty (real space) i0_real_error6.7670e+06
Rg (reciprocal space) rg_reciprocal12.85
I(0) (reciprocal space) i0_reciprocal584600000.0000
Solution quality estimate total_estimate0.6944
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary14.4
Skewness Skewness skewness0.536
Kurtosis Kurtosis kurtosis0.342
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha54660.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.434; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.721; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2jwda2
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
Domain ID domain_idd2jwda3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2jwdA00
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 (1)

9. Files and Curves (10)