MolNFT v1 · #15002 · protein

Structure of the mt-adprase in complex with 1 MN2+ ion and AMP-cp (a inhibitor), a nudix enzyme

1MR2 · Adpr pyrophosphatase: “Structure of the mt-adprase in complex with 1 MN2+ ion and AMP-cp (a inhibitor), a nudix enzyme”. X-ray diffraction, 2 ligands (A12, MN), 2 pockets (best druggability 0.48). MolNFT v1 #15002 on GenesisL1: 3D…

PDB: 1MR2
Type: protein
Length: 187 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: A12, MN
Pockets: 2 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adpr pyrophosphatase (EC 3.6.1.13)	protein	187	21% helix, 41% strand	O33199

Ligands and binding sites

A12 · Phosphomethylphosphonic acid adenosyl ester · ligand · chains A
MN · Manganese (II) 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	213	0.48	0.75	30	MN
2	66	0.34	0.76	20	empty

Compared structures

1MR2 · Structure of the MT-ADPRase in complex with 1 Mn2+ ion and AMP-CP (a inhibitor), a nudix… · 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 1MR2 · PDBe 1MR2 · UniProt O33199

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