4psx

Crystal structure of histone acetyltransferase complex

Method: X-RAY DIFFRACTION Dmax: 148.5 Å Quality: GOOD

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

Histone acetyltransferase type B catalytic subunit

Saccharomyces cerevisiae

UniProt Q12341

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 7–319 Fragment:UNP residues 7-319 Histone acetyltransferase type B subunit 2 × 1 (P39984) Histone H4 × 1 (P02309) Histone H3 × 1 (P61830) COA COENZYME A × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;0.2M potassium sodium tartrate, 20%(w/v) polyethylene glycol 3,350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.51 Å R-free 0.223
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 7–319 Fragment:UNP residues 7-319 Histone acetyltransferase type B subunit 2 × 1 (P39984) Histone H4 × 1 (P02309) Histone H3 × 1 (P61830) COA COENZYME A × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;0.2M potassium sodium tartrate, 20%(w/v) polyethylene glycol 3,350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.51 Å R-free 0.223

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.

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

View Construct and Data Evidence
UniProt name HAT1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–319; UniProt 7–319 Author chain D; PDBConstruct 7–319; UniProt 7–319

Histone acetyltransferase type B subunit 2

Saccharomyces cerevisiae

UniProt P39984

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 B; UniProt 8–389 Fragment:UNP residues 8-389 Mutation:V143T Histone acetyltransferase type B catalytic subunit × 1 (Q12341) Histone H4 × 1 (P02309) Histone H3 × 1 (P61830) COA COENZYME A × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;0.2M potassium sodium tartrate, 20%(w/v) polyethylene glycol 3,350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.51 Å R-free 0.223
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 8–389 Fragment:UNP residues 8-389 Mutation:V143T Histone acetyltransferase type B catalytic subunit × 1 (Q12341) Histone H4 × 1 (P02309) Histone H3 × 1 (P61830) COA COENZYME A × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;0.2M potassium sodium tartrate, 20%(w/v) polyethylene glycol 3,350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.51 Å R-free 0.223

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HAT2_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 8–389; UniProt 8–389 Author chain E; PDBConstruct 8–389; UniProt 8–389

Histone H4

Saccharomyces cerevisiae

UniProt P02309

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 2–49 Fragment:UNP residues 2-49 Mutation:I21V Histone acetyltransferase type B catalytic subunit × 1 (Q12341) Histone acetyltransferase type B subunit 2 × 1 (P39984) Histone H3 × 1 (P61830) COA COENZYME A × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;0.2M potassium sodium tartrate, 20%(w/v) polyethylene glycol 3,350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.51 Å R-free 0.223
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 2–49 Fragment:UNP residues 2-49 Mutation:I21V Histone acetyltransferase type B catalytic subunit × 1 (Q12341) Histone acetyltransferase type B subunit 2 × 1 (P39984) Histone H3 × 1 (P61830) COA COENZYME A × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;0.2M potassium sodium tartrate, 20%(w/v) polyethylene glycol 3,350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.51 Å R-free 0.223

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.

43 other PDB entries and 62 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–48; UniProt 2–49 Author chain F; PDBConstruct 1–48; UniProt 2–49

Histone H3

Saccharomyces cerevisiae S288c

UniProt P61830

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 Y; UniProt 2–16 Fragment:UNP residues 2-16 Histone acetyltransferase type B catalytic subunit × 1 (Q12341) Histone acetyltransferase type B subunit 2 × 1 (P39984) Histone H4 × 1 (P02309) COA COENZYME A × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;0.2M potassium sodium tartrate, 20%(w/v) polyethylene glycol 3,350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.51 Å R-free 0.223
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain P; UniProt 2–16 Fragment:UNP residues 2-16 Histone acetyltransferase type B catalytic subunit × 1 (Q12341) Histone acetyltransferase type B subunit 2 × 1 (P39984) Histone H4 × 1 (P02309) COA COENZYME A × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;0.2M potassium sodium tartrate, 20%(w/v) polyethylene glycol 3,350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.51 Å R-free 0.223

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.

37 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H3_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain P; PDBConstruct 1–15; UniProt 2–16 Author chain Y; PDBConstruct 1–15; UniProt 2–16

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 4psx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4psx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4psx
Deposition date deposition_date2014-03-08
Structure title titleCrystal structure of histone acetyltransferase complex
Keywords keywordsHAT WD40, acetyltransferase, AcCoA, Phosphorylation, HISTONE-TRANSFERASE complex; HISTONE/TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.62
Radius of gyration Rg (electron density) rg_electron43.49
Forward intensity I(0) i0416257000.00
Molecular weight molecular_weight166980.0 kDa
Excluded volume excluded_volume208590 ų
Envelope volume envelope_volume279870 ų
Hydration-shell volume shell_volume55919 ų
Envelope diameter envelope_diameter149.4
Shell Rg shell_rg45.87
Envelope Rg envelope_rg42.99
Shape Rg shape_rg43.49
Total Rg total_rg43.58
Total atoms total_atoms11786
Residues n_residues1446
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 dmax148.5
Rg (real space) rg_real43.75
Rg uncertainty (real space) rg_real_error1.54
I(0) (real space) i0_real4.1630e+08
I(0) uncertainty (real space) i0_real_error8.5170e+06
Rg (reciprocal space) rg_reciprocal43.62
I(0) (reciprocal space) i0_reciprocal416200000.0000
Solution quality estimate total_estimate0.8716
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.6
Skewness Skewness skewness0.359
Kurtosis Kurtosis kurtosis-0.480
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha61090000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.869; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.918; Smooth: 0.802

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4psxa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.108 — Acyl-CoA N-acyltransferases (Nat)
Superfamily Superfamily superfamilyd.108.1 — Acyl-CoA N-acyltransferases (Nat)
Family Family familyd.108.1.1 — N-acetyl transferase, NAT
Domain ID domain_idd4psxb_
Class classb — All beta proteins
Fold Fold foldb.69 — 7-bladed beta-propeller
Superfamily Superfamily superfamilyb.69.4 — WD40 repeat-like
Family Family familyb.69.4.0 — automated matches
Domain ID domain_idd4psxd_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.108 — Acyl-CoA N-acyltransferases (Nat)
Superfamily Superfamily superfamilyd.108.1 — Acyl-CoA N-acyltransferases (Nat)
Family Family familyd.108.1.1 — N-acetyl transferase, NAT
Domain ID domain_idd4psxe_
Class classb — All beta proteins
Fold Fold foldb.69 — 7-bladed beta-propeller
Superfamily Superfamily superfamilyb.69.4 — WD40 repeat-like
Family Family familyb.69.4.0 — automated matches

CATH v4.4 (8 domains)

Domain ID domain_id4psxA01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology360 — Histone Acetyltransferase; domain 1
Homologous superfamily homologous superfamily10 — Histone acetyl transferase 1 (HAT1), N-terminal domain
Domain ID domain_id4psxA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily30 — Gcn5-related N-acetyltransferase (GNAT)
Domain ID domain_id4psxA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily390
Domain ID domain_id4psxB00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id4psxD01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology360 — Histone Acetyltransferase; domain 1
Homologous superfamily homologous superfamily10 — Histone acetyl transferase 1 (HAT1), N-terminal domain
Domain ID domain_id4psxD02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily30 — Gcn5-related N-acetyltransferase (GNAT)
Domain ID domain_id4psxD03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily390
Domain ID domain_id4psxE00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)