3biq

Crystal structure of yeast Spt16 N-terminal Domain

Method: X-RAY DIFFRACTION Dmax: 84.2 Å Quality: GOOD

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

FACT complex subunit SPT16

Saccharomyces cerevisiae

UniProt P32558

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 1–465 Fragment:residues 1-465 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 4.5;298 K;25% Pentaerythritol Ethoxylate (15/4 EO/OH), 100mM Sodium Acetate, pH 4.5, vapor diffusion, temperature 298K Resolution 1.73 Å R-free 0.213

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.

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPT16_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–467; UniProt 1–465

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 3biq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3biq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3biq
Deposition date deposition_date2007-11-30
Structure title titleCrystal structure of yeast Spt16 N-terminal Domain
Keywords keywords;pita-bread, aminopeptidase, chromatin, replication, FACT, Activator, Chromosomal protein, DNA damage, DNA repair, DNA replication, Nucleus, Phosphoprotein, Repressor, Transcription, Transcription regulation ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.91
Radius of gyration Rg (electron density) rg_electron24.07
Forward intensity I(0) i040076800.00
Molecular weight molecular_weight50672.0 kDa
Excluded volume excluded_volume64174 ų
Envelope volume envelope_volume75361 ų
Hydration-shell volume shell_volume26329 ų
Envelope diameter envelope_diameter84.1
Shell Rg shell_rg31.10
Envelope Rg envelope_rg24.27
Shape Rg shape_rg24.06
Total Rg total_rg24.95
Total atoms total_atoms3577
Residues n_residues441
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 dmax84.2
Rg (real space) rg_real24.94
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real4.0080e+07
I(0) uncertainty (real space) i0_real_error6.4280e+05
Rg (reciprocal space) rg_reciprocal24.94
I(0) (reciprocal space) i0_reciprocal40080000.0000
Solution quality estimate total_estimate0.7952
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.398
Kurtosis Kurtosis kurtosis-0.347
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11420000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3biqA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology350 — Creatine Amidinohydrolase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Creatinase/prolidase N-terminal domain
Domain ID domain_id3biqA02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology230 — Creatine Amidinohydrolase
Homologous superfamily homologous superfamily10 — Creatinase/methionine aminopeptidase superfamily

8. Citations (1)

9. Files and Curves (10)