Research workbench
Crystal structure of methyl transferase from methanosarcina acetivorans at 1.6 ångströms resolution, northeast structural genomics consortium (nesg) target MVR53.
Analyse Crystal structure of methyl transferase from methanosarcina acetivorans at 1.6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MRO
- Type
- protein
- Length
- 195 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8TNZ0
- Ligands
- CA, CL
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 195 | — | Q8TNZ0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6MRO · Crystal structure of methyl transferase from Methanosarcina acetivorans at 1.6 Angstroms… · the same entry in another collection · chain A against A, TM-score 0.99
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 Q8TNZ0
- Elsewhere: RCSB PDB 6MRO · PDBe 6MRO · UniProt Q8TNZ0
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