5edu

Crystal structure of human histone deacetylase 6 catalytic domain 2 in complex with trichostatin A

Method: X-RAY DIFFRACTION Dmax: 135.1 Å Quality: GOOD

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

Maltose-binding periplasmic protein, Histone deacetylase 6 chimera

Homo sapiens

UniProt P0AEY0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 27–392 Fragment:MBP + HD6 catalytic domain 2 (UNP residues 479-835) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 TSN TRICHOSTATIN A × 1 ZN ZINC ION × 1 K POTASSIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.2 M potassium sodium tartrate, 20% PEG3350 Resolution 2.79 Å R-free 0.275
2 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–392 Fragment:MBP + HD6 catalytic domain 2 (UNP residues 479-835) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 TSN TRICHOSTATIN A × 1 ZN ZINC ION × 1 K POTASSIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.2 M potassium sodium tartrate, 20% PEG3350 Resolution 2.79 Å R-free 0.275

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.

109 other PDB entries and 147 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECO57
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 19–384; UniProt 27–392 Author chain B; PDBConstruct 19–384; UniProt 27–392

Maltose-binding periplasmic protein, Histone deacetylase 6 chimera

Homo sapiens

UniProt Q9UBN7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 479–835 Fragment:MBP + HD6 catalytic domain 2 (UNP residues 479-835) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 TSN TRICHOSTATIN A × 1 ZN ZINC ION × 1 K POTASSIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.2 M potassium sodium tartrate, 20% PEG3350 Resolution 2.79 Å R-free 0.275
2 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 479–835 Fragment:MBP + HD6 catalytic domain 2 (UNP residues 479-835) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 TSN TRICHOSTATIN A × 1 ZN ZINC ION × 1 K POTASSIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.2 M potassium sodium tartrate, 20% PEG3350 Resolution 2.79 Å R-free 0.275

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 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HDAC6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 389–745; UniProt 479–835 Author chain B; PDBConstruct 389–745; UniProt 479–835

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 5edu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5edu
Deposition date deposition_date2015-10-22
Structure title titleCrystal structure of human histone deacetylase 6 catalytic domain 2 in complex with trichostatin A
Keywords keywordsHYDROLASE-HYDROLASE INHIBITOR complex; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.86
Radius of gyration Rg (electron density) rg_electron41.41
Forward intensity I(0) i0368745000.00
Molecular weight molecular_weight157720.0 kDa
Excluded volume excluded_volume197270 ų
Envelope volume envelope_volume254130 ų
Hydration-shell volume shell_volume52020 ų
Envelope diameter envelope_diameter137.0
Shell Rg shell_rg45.43
Envelope Rg envelope_rg40.71
Shape Rg shape_rg41.40
Total Rg total_rg41.63
Total atoms total_atoms11106
Residues n_residues1443
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 dmax135.1
Rg (real space) rg_real41.93
Rg uncertainty (real space) rg_real_error1.43
I(0) (real space) i0_real3.6870e+08
I(0) uncertainty (real space) i0_real_error7.9940e+06
Rg (reciprocal space) rg_reciprocal41.87
I(0) (reciprocal space) i0_reciprocal368700000.0000
Solution quality estimate total_estimate0.8828
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.8
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.629
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha65440000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.934; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.698

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5eduA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology800 — Arginase; Chain A
Homologous superfamily homologous superfamily20 — Histone deacetylase domain
Domain ID domain_id5eduB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology800 — Arginase; Chain A
Homologous superfamily homologous superfamily20 — Histone deacetylase domain

8. Citations (1)

9. Files and Curves (10)