MolNFT v1 · #180288 · protein

Crystal structure of danio rerio histone deacetylase 10 H137A mutant in complex with N-acetylputrescine (tetrahedral intermediate)

7KUT: “Crystal structure of danio rerio histone deacetylase 10 H137A mutant in complex with N-acetylputrescine…”. X-ray diffraction, 5 ligands (X51, K, ZN). MolNFT v1 #180288 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7KUT
Type: protein
Length: 643 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: F1QCV2
Ligands: X51, K, ZN, NA, PO4

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	643	—	F1QCV2

Ligands and binding sites

X51 · 1-[(4-aminobutyl)amino]ethane-1,1-diol · ligand · chains A
K · Potassium ion · metal · 2 copies · chains A
ZN · Zinc ion · metal · chains A
NA · Sodium ion · metal
PO4 · Phosphate ion · ion · 4 copies · chains A
EDO · 1,2-ethanediol · additive · 7 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

7KUT · Crystal Structure of Danio rerio Histone Deacetylase 10 H137A Mutant in Complex with… · the same entry in another collection · chain A against A, TM-score 1.00
F1QCV2 · AlphaFold monomer V2.0 prediction for polyamine deacetylase HDAC10 (F1QCV2) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt F1QCV2
Elsewhere: RCSB PDB 7KUT · PDBe 7KUT · UniProt F1QCV2

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