1eo0

CONSERVED DOMAIN COMMON TO TRANSCRIPTION FACTORS TFIIS, ELONGIN A, CRSP70

Method: SOLUTION NMR Dmax: 40.5 Å Quality: GOOD

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

TRANSCRIPTION ELONGATION FACTOR S-II

Saccharomyces cerevisiae

UniProt P07273

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 1–77 Fragment:DOMAIN I No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.5;273 K;Ionic strength (raw mmCIF value) 300 mM NaCl;Pressure ambient NMR sample composition:2 mM TFIIS1-111; 10 mM phosphate buffer; 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.

13 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TFS2_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–77; UniProt 1–77

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 1eo0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1eo0
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1eo0
Deposition date deposition_date2000-03-21
Structure title titleCONSERVED DOMAIN COMMON TO TRANSCRIPTION FACTORS TFIIS, ELONGIN A, CRSP70
Keywords keywordshelix-bundle, Structural Genomics, PSI, Protein Structure Initiative, Northeast Structural Genomics Consortium, NESG, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.86
Radius of gyration Rg (electron density) rg_electron11.57
Forward intensity I(0) i099257500.00
Molecular weight molecular_weight88084.0 kDa
Excluded volume excluded_volume112700 ų
Envelope volume envelope_volume15258 ų
Hydration-shell volume shell_volume10414 ų
Envelope diameter envelope_diameter41.0
Shell Rg shell_rg18.18
Envelope Rg envelope_rg12.92
Shape Rg shape_rg11.52
Total Rg total_rg12.02
Total atoms total_atoms12840
Residues n_residues770
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 dmax40.5
Rg (real space) rg_real11.83
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real9.9260e+07
I(0) uncertainty (real space) i0_real_error1.0920e+06
Rg (reciprocal space) rg_reciprocal11.83
I(0) (reciprocal space) i0_reciprocal99260000.0000
Solution quality estimate total_estimate0.8406
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.8
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.171
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha105600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.644; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.991

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_idd1eo0a_
Class classa — All alpha proteins
Fold Fold folda.48 — N-cbl like
Superfamily Superfamily superfamilya.48.3 — Conserved domain common to transcription factors TFIIS, elongin A, CRSP70
Family Family familya.48.3.1 — Conserved domain common to transcription factors TFIIS, elongin A, CRSP70

CATH v4.4 (1 domains)

Domain ID domain_id1eo0A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology930 — Transcription Elongation Factor S-II; Chain A
Homologous superfamily homologous superfamily10 — Conserved domain common to transcription factors TFIIS, elongin A, CRSP70

8. Citations (1)

9. Files and Curves (10)