MolNFT v1 · #14934 · protein
Structure of mt-adprase (apoenzyme), a nudix hydrolase from mycobacterium tuberculosis
1MP2 · Adpr pyrophosphatase: “Structure of mt-adprase (apoenzyme), a nudix hydrolase from mycobacterium tuberculosis”. X-ray diffraction, 1 pocket (best druggability 0.50). MolNFT v1 #14934 on GenesisL1: 3D structure, binding sites and…
- 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.
| Volume (ų) | 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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