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E.coli NAD Synthetase, AMP

Analyse E.coli NAD Synthetase, AMP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WXE
Type: protein
Length: 258 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.9
Source: Escherichia coli
Molecule: NH(3)-dependent NAD(+) synthetase
EC: 6.3.1.5
UniProt: P18843
Ligands: AMP, MG
Pockets: 2 · best druggability 0.59

Structure

x-ray diffraction · resolution 1.9 · 1 distinct chain · 54% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NH(3)-dependent NAD(+) synthetase (EC 6.3.1.5)	protein	258	54% helix, 8% strand	P18843

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · 2 copies · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	361	0.59	0.77	48	MG, AMP
2	84	0.37	0.76	23	empty

Compared structures

1WXE · E.COLI NAD synthetase, AMP · the same entry in another collection · chain A against A, TM-score 1.00
P18843 · AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (P18843) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P18843
Elsewhere: RCSB PDB 1WXE · PDBe 1WXE · UniProt P18843

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