MolNFT v2 · #4245 · protein

Crystal structure of the NAD complex of human deoxyhypusine synthase

1DHS: “Crystal structure of the NAD complex of human deoxyhypusine synthase”. X-ray diffraction at 2.2, 1 ligand (NAD), 1 pocket (best druggability 0.43). MolNFT v2 #4245 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1DHS
Type: protein
Length: 344 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.2
Source: Homo sapiens
Molecule: Deoxyhypusine synthase
EC: 2.5.1.46
UniProt: P49366
Ligands: NAD
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · resolution 2.2 · 1 distinct chain · 51% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Deoxyhypusine synthase (EC 2.5.1.46)	protein	344	51% helix, 11% strand	P49366

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	112	0.43	0.77	20	empty

Compared structures

1DHS · Crystal structure of the NAD complex of human deoxyhypusine synthase · the same entry in another collection · chain A against A, TM-score 1.00
P49366 · AlphaFold monomer V2.0 prediction for deoxyhypusine synthase (P49366) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P49366
Elsewhere: RCSB PDB 1DHS · PDBe 1DHS · UniProt P49366

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