1b8x

GLUTATHIONE S-TRANSFERASE FUSED WITH THE NUCLEAR MATRIX TARGETING SIGNAL OF THE TRANSCRIPTION FACTOR AML-1

Method: X-RAY DIFFRACTION Dmax: 82.0 Å Quality: GOOD

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

PROTEIN (AML-1B)

Escherichia coli

UniProt P08515

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 1–280 Fragment:NMTS FRAGMENT No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;pH 7.5 Resolution 2.70 Å R-free 0.310
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–280 Fragment:NMTS FRAGMENT No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;pH 7.5 Resolution 2.70 Å R-free 0.310

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.

64 other PDB entries and 69 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GST26_SCHJA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–280; UniProt 1–280

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 1b8x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1b8x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1b8x
Deposition date deposition_date1999-02-03
Structure title titleGLUTATHIONE S-TRANSFERASE FUSED WITH THE NUCLEAR MATRIX TARGETING SIGNAL OF THE TRANSCRIPTION FACTOR AML-1
Keywords keywordsNUCLEAR MATRIX TARGETING SIGNAL PROTEIN, SIGNAL PROTEIN; SIGNAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.06
Radius of gyration Rg (electron density) rg_electron20.74
Forward intensity I(0) i014857500.00
Molecular weight molecular_weight29611.0 kDa
Excluded volume excluded_volume37394 ų
Envelope volume envelope_volume47969 ų
Hydration-shell volume shell_volume19884 ų
Envelope diameter envelope_diameter83.9
Shell Rg shell_rg26.64
Envelope Rg envelope_rg22.12
Shape Rg shape_rg20.67
Total Rg total_rg21.83
Total atoms total_atoms2083
Residues n_residues260
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 dmax82.0
Rg (real space) rg_real22.19
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real1.4860e+07
I(0) uncertainty (real space) i0_real_error2.2500e+05
Rg (reciprocal space) rg_reciprocal22.16
I(0) (reciprocal space) i0_reciprocal14860000.0000
Solution quality estimate total_estimate0.8101
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.7
Skewness Skewness skewness0.589
Kurtosis Kurtosis kurtosis0.324
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3454000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.580; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.799; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1b8xa1
Class classa — All alpha proteins
Fold Fold folda.45 — GST C-terminal domain-like
Superfamily Superfamily superfamilya.45.1 — GST C-terminal domain-like
Family Family familya.45.1.1 — Glutathione S-transferase (GST), C-terminal domain
Domain ID domain_idd1b8xa2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.5 — Glutathione S-transferase (GST), N-terminal domain

CATH v4.4 (3 domains)

Domain ID domain_id1b8xA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id1b8xA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily10
Domain ID domain_id1b8xA03
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology770 — Signal Protein Aml-1b; Chain A, domain 3
Homologous superfamily homologous superfamily10 — Signal Protein Aml-1b; Chain A, domain 3

8. Citations (1)

9. Files and Curves (10)