← Back to search
1r4t

Solution structure of exoenzyme S

Method: SOLUTION NMR Dmax: 49.6 Å Quality: GOOD
▼

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

exoenzyme S

Pseudomonas aeruginosa

UniProt Q93SQ1

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 96–234 Fragment：GAP-DOMAIN (RESIDUES 96-234) No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7.4；298 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient NMR sample composition：0.5-1.2 mM exos [U-95% 13C; U-90% 15N]50mM phosphate buffer | 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.

Other PDB Difference from Current Entry 1R4T Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6GN8 Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, trimeric crystal form Deposited 2018-05-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 233–453（221 aa）
Mutation：E379A, E381A MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；40% MPD, 8% PEG 8000, 0.1M Sodium Cacodylate
Resolution 2.34 Å R-free 0.248
6GNJ Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, trimeric crystal form in complex with STO1101 Deposited 2018-05-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 233–453（221 aa）
Mutation：E379A, E381A F4W 3-(12-oxidanylidene-7-thia-9,11-diazatricyclo[6.4.0.0^{2,6}]dodeca-1(8),2(6),9-trien-10-yl)propanoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；40% MPD, 7% PEG 8000, 0.1M Sodium Cacodylate
Resolution 3.24 Å R-free 0.221
6GNK Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, trimeric crystal form bound to Carba-NAD Deposited 2018-05-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 233–453（221 aa）
Mutation：E379A, E381A CNA CARBA-NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；50% MPD, 8% PEG 8000, 0.1M Sodium Cacodylate
Resolution 2.55 Å R-free 0.239

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q93SQ1_PSEAE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 4–142； UniProt 96–234

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 1r4t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1r4t
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1r4t
Deposition date deposition_date2003-10-08
Structure title titleSolution structure of exoenzyme S
Keywords keywordsEXOS, PSEUDOMONAS AERUGINOSA, GAP, TOXIN, VIRULENCE FACTOR, SIGNAL TRANSDUCTION; TOXIN
Experimental Method methodSOLUTION NMR
▼

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

Radius of gyration Rg (Guinier) rg_guinier14.39 Å
Radius of gyration Rg (electron density) rg_electron14.15 Å
Forward intensity I(0) i01333300000.00
Molecular weight molecular_weight295950.0 kDa
Excluded volume excluded_volume366060 ų
Envelope volume envelope_volume25141 ų
Hydration-shell volume shell_volume13764 ų
Envelope diameter envelope_diameter54.9 Å
Shell Rg shell_rg21.42 Å
Envelope Rg envelope_rg16.32 Å
Shape Rg shape_rg14.14 Å
Total Rg total_rg14.28 Å
Total atoms total_atoms41998
Residues n_residues2806
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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 Å
Rg (real space) rg_real14.43 Å
Rg uncertainty (real space) rg_real_error0.39 Å
I(0) (real space) i0_real1.3330e+09
I(0) uncertainty (real space) i0_real_error1.5280e+07
Rg (reciprocal space) rg_reciprocal14.43 Å
I(0) (reciprocal space) i0_reciprocal1333000000.0000
Solution quality estimate total_estimate0.7595
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary16.3 Å
Skewness Skewness skewness0.482
Kurtosis Kurtosis kurtosis0.065
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha358900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.637; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; 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_idd1r4ta_
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.11 — Bacterial GAP domain
Family Family familya.24.11.1 — Bacterial GAP domain

CATH v4.4 (1 domains)

Domain ID domain_id1r4tA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily260 — Virulence factor YopE uncharacterised domain
▶

8. Citations (1)

▶

9. Files and Curves (10)