MolNFT v1 · #163987 · protein
Methyltransferase of the mtga N227A mutant from desulfitobacterium hafniense
6SJP · Tetrahydromethanopterin S-methyltransferase: “Methyltransferase of the mtga N227A mutant from desulfitobacterium hafniense”. X-ray diffraction, 7 pockets (best druggability 0.63). MolNFT v1 #163987 on GenesisL1: 3D structure…
- PDB
- 6SJP
- Type
- protein
- Length
- 610 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetrahydromethanopterin S-methyltransferase
- EC
- 2.1.1.86
- UniProt
- B8FUR2
- Pockets
- 7 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tetrahydromethanopterin S-methyltransferase (EC 2.1.1.86) | protein | 305 | 46% helix, 19% strand | B8FUR2 |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 390 | 0.63 | 0.78 | 32 | empty |
| 2 | 407 | 0.61 | 0.76 | 35 | empty |
| 3 | 198 | 0.60 | 0.81 | 33 | empty |
| 4 | 110 | 0.43 | 0.77 | 15 | empty |
| 5 | 86 | 0.34 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1990 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 6SJP · Methyltransferase of the MtgA N227A mutant from Desulfitobacterium hafniense · 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 B8FUR2
- Elsewhere: RCSB PDB 6SJP · PDBe 6SJP · UniProt B8FUR2
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