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The E41Q mutant of the amidase from nesterenkonia sp. AN1 showing covalent addition of the acetamide moiety of fluoroacetamide at the active site cysteine

Analyse The E41Q mutant of the amidase from nesterenkonia sp. AN1 showing covalent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4IZT
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amidase
EC: 3.5.1.4
UniProt: D0VWZ1
Ligands: FTM, ACM
Pockets: 2 · best druggability 0.42

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amidase (EC 3.5.1.4)	protein	263	33% helix, 28% strand	D0VWZ1

Ligands and binding sites

FTM · 2-fluoroacetamide · ligand · 2 copies · chains A
ACM · Acetamide · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	90	0.42	0.78	22	ACM, FTM
2	61	0.28	0.74	13	empty

Modifications

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

Compared structures

4IZT · The E41Q mutant of the amidase from Nesterenkonia sp. AN1 showing covalent addition of… · 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 D0VWZ1
Elsewhere: RCSB PDB 4IZT · PDBe 4IZT · UniProt D0VWZ1

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