MolNFT v1 · #119419 · protein

Crystal structure of tact (tRNA acetylating toxin) from salmonella

5FVJ · Putative acetyltransferase: “Crystal structure of tact (tRNA acetylating toxin) from salmonella”. X-ray diffraction, 1 ligand (ACO), 2 pockets (best druggability 0.64). MolNFT v1 #119419 on GenesisL1: 3D structure, binding sites and…

PDB: 5FVJ
Type: protein
Length: 323 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative acetyltransferase
UniProt: E8XFW6
Ligands: ACO
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative acetyltransferase	protein	165	32% helix, 29% strand	E8XFW6
B	Putative acetyltransferase	protein	158	33% helix, 29% strand	E8XFW6

Ligands and binding sites

ACO · Acetyl coenzyme *A · ligand · 2 copies · chains A, B

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

Pockets

2 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	421	0.64	0.78	52	ACO
2	366	0.64	0.78	49	ACO

Interfaces

1 interface between chains.

A–B · 1253 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

5FVJ · Crystal structure of TacT (tRNA acetylating toxin) from Salmonella · 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 E8XFW6
Elsewhere: RCSB PDB 5FVJ · PDBe 5FVJ · UniProt E8XFW6

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