MolNFT v1 · #71380 · protein
Crystal structure of the 6-hyroxymethyl-7,8-dihydropterin pyrophosphokinase dihydropteroate synthase bifunctional enzyme from francisella tularensis
3MCM · 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine…: “Crystal structure of the 6-hyroxymethyl-7,8-dihydropterin pyrophosphokinase dihydropteroate synthase…”. X-ray diffraction, 1 ligand (MG), 8 pockets (best druggability 0.65).…
- PDB
- 3MCM
- Type
- protein
- Length
- 745 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine PYROPHOSPHOKINASE/DIHYDROPTEROATE…
- UniProt
- Q2A2W3
- Ligands
- MG
- Pockets
- 8 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine PYROPHOSPHOKINASE/DIHYDROPTEROATE synthase | protein | 368 | 39% helix, 21% strand | Q2A2W3 |
| B | 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine PYROPHOSPHOKINASE/DIHYDROPTEROATE synthase | protein | 377 | 44% helix, 22% strand | Q2A2W3 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 426 | 0.65 | 0.79 | 40 | empty |
| 2 | 420 | 0.65 | 0.79 | 40 | empty |
| 3 | 206 | 0.52 | 0.77 | 23 | empty |
| 4 | 173 | 0.51 | 0.78 | 23 | empty |
| 5 | 51 | 0.45 | 0.85 | 18 | empty |
Compared structures
- 3MCM · Crystal Structure of the 6-hyroxymethyl-7,8-dihydropterin pyrophosphokinase… · 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 Q2A2W3
- Elsewhere: RCSB PDB 3MCM · PDBe 3MCM · UniProt Q2A2W3
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