MolNFT v1 · #94475 · protein

Crystal structure of 3'(2'),5'-bisphosphate NUCLEOTIDASE1 from entamoeba histolytica in complex with AMP and metal ions

4HXV · 3'(2'),5'-bisphosphate nucleotidase, putative: “Crystal structure of 3'(2'),5'-bisphosphate NUCLEOTIDASE1 from entamoeba histolytica in complex with AMP and…”. X-ray diffraction, 3 ligands (AMP, MG, NA), 1 pocket (best druggability…

PDB: 4HXV
Type: protein
Length: 317 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3'(2'),5'-bisphosphate nucleotidase, putative
EC: 3.1.3.7
UniProt: C4M4T9
Ligands: AMP, MG, NA
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3'(2'),5'-bisphosphate nucleotidase, putative (EC 3.1.3.7)	protein	317	34% helix, 23% strand	C4M4T9

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
NA · Sodium ion · metal · 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	275	0.65	0.82	41	MG, AMP, NA

Compared structures

4HXV · Crystal structure of 3'(2'),5'-bisphosphate nucleotidase1 from Entamoeba histolytica in… · 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 C4M4T9
Elsewhere: RCSB PDB 4HXV · PDBe 4HXV · UniProt C4M4T9

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