MolNFT v1 · #63894 · protein

Crystal structure of a putative acetyltransferase from listeria innocua

3FNC: “Crystal structure of a putative acetyltransferase from listeria innocua”. X-ray diffraction, 2 pockets (best druggability 0.84). MolNFT v1 #63894 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3FNC
Type: protein
Length: 321 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative acetyltransferase
UniProt: Q92E50
Pockets: 2 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative acetyltransferase	protein	160	39% helix, 36% strand	Q92E50
B	Putative acetyltransferase	protein	161	40% helix, 35% strand	Q92E50

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 9 copies · chains A, B
MLI · Malonate ion · additive · 3 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	850	0.84	0.86	79	MLI, EDO
2	552	0.72	0.80	61	EDO, MLI

Interfaces

1 interface between chains.

A–B · 678 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

3FNC · Crystal structure of a putative acetyltransferase from Listeria innocua · 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 Q92E50
Elsewhere: RCSB PDB 3FNC · PDBe 3FNC · UniProt Q92E50

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