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Deoxyhypusine synthase holoenzyme in its high ionic strength, low pH crystal form

Analyse Deoxyhypusine synthase holoenzyme in its high ionic strength, low pH crystal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RLZ
Type: protein
Length: 344 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Deoxyhypusine synthase
EC: 2.5.1.46
UniProt: P49366
Ligands: NAD
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Deoxyhypusine synthase (EC 2.5.1.46)	protein	344	51% helix, 12% 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	109	0.42	0.77	21	empty

Compared structures

1RLZ · Deoxyhypusine synthase holoenzyme in its high ionic strength, low pH crystal form · 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 1RLZ · PDBe 1RLZ · UniProt P49366

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