Research workbench

Crystal structure of leishmania major N- myristoyltransferase (nmt) with bound myristoyl-CoA and a thiazolidinone ligand

Analyse Crystal structure of leishmania major N- myristoyltransferase (nmt) with bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5AG4
Type: protein
Length: 411 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycylpeptide N-tetradecanoyltransferase
EC: 2.3.1.97
UniProt: Q4Q5S8
Ligands: MYA, N8N
Pockets: 3 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97)	protein	411	32% helix, 28% strand	Q4Q5S8

Ligands and binding sites

MYA · Tetradecanoyl-coa · ligand · chains A
N8N · (2S)-3-(3-chlorophenyl)-2-(pyridin-2-yl)-1,3-thiazolidin-4-one · ligand · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	956	0.79	0.81	92	MYA, N8N
2	62	0.72	0.98	24	empty
3	119	0.41	0.75	23	empty

Compared structures

5AG4 · Crystal structure of leishmania major N-myristoyltransferase (nmt) with bound… · the same entry in another collection · 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 Q4Q5S8
Elsewhere: RCSB PDB 5AG4 · PDBe 5AG4 · UniProt Q4Q5S8

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.