Research workbench
Crystal structure of methyltransferase mboiia (moraxella bovis)
Analyse Crystal structure of methyltransferase mboiia (moraxella bovis) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G60
- Type
- protein
- Length
- 466 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenine-specific methyltransferase mboiia
- EC
- 2.1.1.72
- UniProt
- P23192
- Ligands
- SAM, NA
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenine-specific methyltransferase mboiia (EC 2.1.1.72) | protein | 238 | 36% helix, 22% strand | P23192 |
| B | Adenine-specific methyltransferase mboiia (EC 2.1.1.72) | protein | 228 | 33% helix, 25% strand | P23192 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 473 | 0.71 | 0.81 | 61 | NA, SAM |
| 2 | 496 | 0.67 | 0.78 | 58 | NA, SAM |
| 3 | 318 | 0.64 | 0.80 | 42 | empty |
| 4 | 259 | 0.61 | 0.80 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 1984 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 1G60 · Crystal Structure of Methyltransferase MboIIa (Moraxella bovis) · the same entry in another collection · chain A against A, TM-score 1.00
- P23192 · AlphaFold monomer V2.0 prediction for modification methylase mboii (P23192) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P23192
- Elsewhere: RCSB PDB 1G60 · PDBe 1G60 · UniProt P23192
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