MolNFT v1 · #14996 · protein

Structure of the mt-adprase in complex with three MN2+ ions and ampcpr, a nudix enzyme

1MQW · Adpr pyrophosphatase: “Structure of the mt-adprase in complex with three MN2+ ions and ampcpr, a nudix enzyme”. X-ray diffraction, 2 ligands (ADV, MN), 1 pocket (best druggability 0.55). MolNFT v1 #14996 on GenesisL1: 3D structure…

PDB: 1MQW
Type: protein
Length: 200 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adpr pyrophosphatase
EC: 3.6.1.13
UniProt: O33199
Ligands: ADV, MN
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adpr pyrophosphatase (EC 3.6.1.13)	protein	200	23% helix, 41% strand	O33199

Ligands and binding sites

ADV · Alpha-beta methylene adp-ribose · ligand · chains A
MN · Manganese (II) ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	301	0.55	0.75	39	MN, ADV

Compared structures

1MQW · Structure of the MT-ADPRase in complex with three Mn2+ ions and AMPCPR, a Nudix enzyme · 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 O33199
Elsewhere: RCSB PDB 1MQW · PDBe 1MQW · UniProt O33199

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