MolNFT v1 · #26711 · protein

E.COLI NAD synthetase, AMP.PP

1WXI · NH(3)-dependent NAD(+) synthetase: “E.COLI NAD synthetase, AMP.PP”. X-ray diffraction, 3 ligands (AMP, DPO, MG), 2 pockets (best druggability 0.65). MolNFT v1 #26711 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1WXI
Type: protein
Length: 261 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NH(3)-dependent NAD(+) synthetase
EC: 6.3.1.5
UniProt: P18843
Ligands: AMP, DPO, MG
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NH(3)-dependent NAD(+) synthetase (EC 6.3.1.5)	protein	261	55% helix, 8% strand	P18843

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · 2 copies · chains A
DPO · Diphosphate · ligand · chains A
MG · Magnesium ion · metal · 2 copies · 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	484	0.65	0.77	57	MG, AMP, DPO
2	91	0.37	0.75	24	empty

Compared structures

1WXI · E.coli NAD Synthetase, AMP.PP · 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 1WXI · PDBe 1WXI · UniProt P18843

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