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Crystal structure of leishmania major N-myristoyltransferase with bound myristoyl-CoA

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

PDB: 3H5Z
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, UNX
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97)	protein	411	33% helix, 28% strand	Q4Q5S8

Ligands and binding sites

MYA · Tetradecanoyl-coa · ligand · chains A
UNX · Unknown atom or ion · ion · 11 copies · chains A
EDO · 1,2-ethanediol · additive · 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	1030	0.78	0.80	91	MYA, EDO, UNX
2	125	0.42	0.76	22	empty

Compared structures

3H5Z · Crystal Structure of Leishmania major N-myristoyltransferase with bound myristoyl-CoA · 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 3H5Z · PDBe 3H5Z · UniProt Q4Q5S8

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