MolNFT v1 · #98394 · protein

Crystal structure of a gnat superfamily acetyltransferase PA4794 in ternary complex with N-phenylacetyl-gly-aclys and CoA

4L8A · Uncharacterized protein: “Crystal structure of a gnat superfamily acetyltransferase PA4794 in ternary complex with…”. X-ray diffraction, 3 ligands (COA, 1VP, SO4), 1 pocket (best druggability 0.69). MolNFT v1 #98394 on GenesisL1: 3D…

PDB: 4L8A
Type: protein
Length: 159 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: Q9HV14
Ligands: COA, 1VP, SO4
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	159	34% helix, 37% strand	Q9HV14

Ligands and binding sites

COA · Coenzyme A · ligand · chains A
1VP · N-(phenylacetyl)glycyl-N~6~-acetyl-L-lysine · ligand · chains A
SO4 · Sulfate ion · ion · 5 copies · chains A
EDO · 1,2-ethanediol · additive · 6 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	381	0.69	0.81	45	COA, SO4, 1VP

Compared structures

4L8A · Crystal structure of a GNAT superfamily acetyltransferase PA4794 in ternary complex with… · 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 Q9HV14
Elsewhere: RCSB PDB 4L8A · PDBe 4L8A · UniProt Q9HV14

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