MolNFT v1 · #139927 · protein

Crystal structure of Y145F mutant of kact

5XUN · Acetyltransferase: “Crystal structure of Y145F mutant of kact”. X-ray diffraction, 1 ligand (ACO), 3 pockets (best druggability 0.70). MolNFT v1 #139927 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5XUN
Type: protein
Length: 341 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyltransferase
UniProt: A0A081LU80
Ligands: ACO
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyltransferase	protein	170	36% helix, 29% strand	A0A081LU80
B	Acetyltransferase	protein	171	36% helix, 29% strand	A0A081LU80

Ligands and binding sites

ACO · Acetyl coenzyme *A · ligand · 2 copies · chains A, B
ACT · Acetate ion · additive · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	451	0.70	0.80	48	ACO
2	268	0.64	0.81	29	ACO
3	205	0.57	0.79	27	empty

Interfaces

1 interface between chains.

A–B · 1146 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

5XUN · Crystal structure of Y145F mutant of KacT · 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 A0A081LU80
Elsewhere: RCSB PDB 5XUN · PDBe 5XUN · UniProt A0A081LU80

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