Research workbench

Acinetobacter baumanii nicotinamidase pyrazinamidease

Analyse Acinetobacter baumanii nicotinamidase pyrazinamidease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WTA
Type: protein
Length: 212 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nicotinamidase
EC: 3.5.1.19
UniProt: B0VA03
Ligands: VGL, ZN, CL
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nicotinamidase (EC 3.5.1.19)	protein	212	28% helix, 25% strand	B0VA03

Ligands and binding sites

VGL · Pyrazine-2-carboxylic acid · ligand · chains A
ZN · Zinc ion · metal · chains A
CL · Chloride ion · ion · 3 copies · chains A
GOL · Glycerol · additive · 3 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	74	0.34	0.75	21	GOL

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2WTA · Acinetobacter baumanii nicotinamidase pyrazinamidease · 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 B0VA03
Elsewhere: RCSB PDB 2WTA · PDBe 2WTA · UniProt B0VA03

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.