5bt1

histone chaperone Hif1 playing with histone H2A-H2B dimer

Method: X-RAY DIFFRACTION Dmax: 105.0 Å Quality: GOOD

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

HAT1-interacting factor 1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt Q12373

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–385 Chain B; UniProt 1–385 Not recorded Histone H2A.1 × 1 (P04911) Histone H2B.1 × 1 (P02293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;0.1M Magnesium formate dihydrate, 15% PEG3350 Resolution 2.62 Å R-free 0.262

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HIF1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–385; UniProt 1–385 Author chain B; PDBConstruct 1–385; UniProt 1–385

Histone H2A.1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P04911

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–132 Not recorded HAT1-interacting factor 1 × 2 (Q12373) Histone H2B.1 × 1 (P02293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;0.1M Magnesium formate dihydrate, 15% PEG3350 Resolution 2.62 Å R-free 0.262

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.

20 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 12–143; UniProt 1–132

Histone H2B.1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P02293

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–131 Not recorded HAT1-interacting factor 1 × 2 (Q12373) Histone H2A.1 × 1 (P04911) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;0.1M Magnesium formate dihydrate, 15% PEG3350 Resolution 2.62 Å R-free 0.262

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.

23 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 12–142; UniProt 1–131

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 5bt1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5bt1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5bt1
Deposition date deposition_date2015-06-02
Structure title titlehistone chaperone Hif1 playing with histone H2A-H2B dimer
Keywords keywordsHistone chaperone complex, TPR, NASP homolog, assembly, CHAPERONE; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.32
Radius of gyration Rg (electron density) rg_electron30.68
Forward intensity I(0) i089911200.00
Molecular weight molecular_weight74817.0 kDa
Excluded volume excluded_volume93698 ų
Envelope volume envelope_volume122130 ų
Hydration-shell volume shell_volume34001 ų
Envelope diameter envelope_diameter110.1
Shell Rg shell_rg37.02
Envelope Rg envelope_rg30.73
Shape Rg shape_rg30.65
Total Rg total_rg31.32
Total atoms total_atoms5270
Residues n_residues668
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 dmax105.0
Rg (real space) rg_real31.40
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real8.9910e+07
I(0) uncertainty (real space) i0_real_error1.4170e+06
Rg (reciprocal space) rg_reciprocal31.37
I(0) (reciprocal space) i0_reciprocal89910000.0000
Solution quality estimate total_estimate0.8849
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.380
Kurtosis Kurtosis kurtosis-0.422
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15640000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.918; Smooth: 0.958

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5bt1c_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd5bt1d_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones

CATH v4.4 (4 domains)

Domain ID domain_id5bt1A00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain
Domain ID domain_id5bt1B00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain
Domain ID domain_id5bt1C00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id5bt1D00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A

8. Citations (1)

9. Files and Curves (10)