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Structure of mt-adprase (apoenzyme), a nudix hydrolase from mycobacterium tuberculosis

Analyse Structure of mt-adprase (apoenzyme), a nudix hydrolase from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MP2
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
Pockets: 1 · best druggability 0.50

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	237	0.50	0.74	30	empty

Compared structures

1MP2 · Structure of MT-ADPRase (Apoenzyme), a Nudix hydrolase from Mycobacterium tuberculosis · 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 1MP2 · PDBe 1MP2 · UniProt O33199

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