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Structure of the polyamine acetyltransferase DpA

Analyse Structure of the polyamine acetyltransferase DpA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8A9O
Type: protein
Length: 296 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.587
Source: Acinetobacter baumannii
Molecule: DpA polyamine acetyltransferase
UniProt: A0A385EXR5
Ligands: COA, ACO, NA, MG, BR
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · resolution 1.587 · 2 distinct chains · 38% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DpA polyamine acetyltransferase	protein	148	38% helix, 34% strand	A0A385EXR5
B	DpA polyamine acetyltransferase	protein	148	39% helix, 36% strand	A0A385EXR5

Ligands and binding sites

COA · Coenzyme A · ligand · chains A
ACO · Acetyl coenzyme *A · ligand · chains B
NA · Sodium ion · metal · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B
BR · Bromide ion · ion · 18 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	1091	0.80	0.81	88	BR, ACO
2	243	0.59	0.79	27	COA

Interfaces

1 interface between chains.

A–B · 2419 Å² buried · 47 hydrogen bonds · protein-protein

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Every structure of UniProt A0A385EXR5
Elsewhere: RCSB PDB 8A9O · PDBe 8A9O · UniProt A0A385EXR5

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