Research workbench
Helicobacter pylori mtan
Analyse Helicobacter pylori mtan in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NM4
- Type
- protein
- Length
- 451 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MTA/SAH nucleosidase
- EC
- 3.2.2.9
- UniProt
- Q9ZMY2
- Pockets
- 4 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MTA/SAH nucleosidase (EC 3.2.2.9) | protein | 229 | 38% helix, 30% strand | Q9ZMY2 |
| B | MTA/SAH nucleosidase (EC 3.2.2.9) | protein | 222 | 37% helix, 32% strand | Q9ZMY2 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 6 copies · chains A, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.66 | 0.89 | 31 | TRS, EDO |
| 2 | 273 | 0.64 | 0.80 | 31 | EDO |
| 3 | 90 | 0.49 | 0.82 | 19 | empty |
| 4 | 216 | 0.48 | 0.75 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1639 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
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 Q9ZMY2
- Elsewhere: RCSB PDB 3NM4 · PDBe 3NM4 · UniProt Q9ZMY2
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