Research workbench
Crystal structure of the methanosarcina barkeri monomethylamine methyltransferase (mtmb)
Analyse Crystal structure of the methanosarcina barkeri monomethylamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L2Q
- Type
- protein
- Length
- 457 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Monomethylamine methyltransferase
- UniProt
- O30642
- Ligands
- NH4
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Monomethylamine methyltransferase | protein | 457 | 46% helix, 15% strand | O30642 |
Ligands and binding sites
- NH4 · Ammonium ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 229 | 0.51 | 0.76 | 34 | empty |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 1L2Q · Crystal Structure of the Methanosarcina barkeri Monomethylamine Methyltransferase (MtmB) · 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 O30642
- Elsewhere: RCSB PDB 1L2Q · PDBe 1L2Q · UniProt O30642
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