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Crystal structure of the covalent adduct formed between mycobacterium marinum aryalamine N-acetyltransferase and phenyl vinyl ketone a derivative of piperidinols

Analyse Crystal structure of the covalent adduct formed between mycobacterium marinum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4B55
Type: protein
Length: 273 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arylamine N-acetyltransferase nat
EC: 2.3.1.5
UniProt: B2HIZ6
Ligands: P18
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Arylamine N-acetyltransferase nat (EC 2.3.1.5)	protein	273	35% helix, 26% strand	B2HIZ6

Ligands and binding sites

P18 · 3-hydroxy-1-phenylpropan-1-one · 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	410	0.64	0.78	48	P18
2	53	0.43	0.83	13	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

4B55 · Crystal Structure of the Covalent Adduct Formed between Mycobacterium marinum Aryalamine… · 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 B2HIZ6
Elsewhere: RCSB PDB 4B55 · PDBe 4B55 · UniProt B2HIZ6

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