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Diaminobutyrate acetyltransferase ecta from paenibacillus lautus in complex with coenzyme a

Analyse Diaminobutyrate acetyltransferase ecta from paenibacillus lautus in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SK1
Type: protein
Length: 160 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-2,4-diaminobutyric acid acetyltransferase
EC: 2.3.1.178
UniProt: D3EKC1
Ligands: COA
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-2,4-diaminobutyric acid acetyltransferase (EC 2.3.1.178)	protein	160	37% helix, 32% strand	D3EKC1

Ligands and binding sites

COA · Coenzyme A · ligand · chains A
ACT · Acetate ion · additive · 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	452	0.65	0.78	43	COA

Compared structures

6SK1 · Diaminobutyrate acetyltransferase EctA from Paenibacillus lautus in complex with coenzyme… · 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 D3EKC1
Elsewhere: RCSB PDB 6SK1 · PDBe 6SK1 · UniProt D3EKC1

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