MolNFT v1 · #148003 · protein

Leishmania major N-myristoyltransferase with bound myristoyl-CoA and inhibitor

6EU5 · Glycylpeptide N-tetradecanoyltransferase: “Leishmania major N-myristoyltransferase with bound myristoyl-CoA and inhibitor”. X-ray diffraction, 2 ligands (MYA, BXN), 2 pockets (best druggability 0.79). MolNFT v1 #148003 on GenesisL1…

PDB: 6EU5
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, BXN
Pockets: 2 · 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
BXN · 4-[3-[(8~{A}~{R})-3,4,6,7,8,8~{A}-hexahydro-1~{H}-pyrrolo[1,2-a]pyrazin-2-yl]propyl]-2,6-bis(chloranyl)-~{N}-methyl-~{N}-(1,3,5-trimethylpyrazol-4-yl) benzenesulfonamide · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	987	0.79	0.81	91	MYA, BXN
2	112	0.41	0.76	26	empty

Compared structures

6EU5 · Leishmania major N-myristoyltransferase with bound myristoyl-CoA and inhibitor · 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 6EU5 · PDBe 6EU5 · UniProt Q4Q5S8

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