MolNFT v1 · #106308 · protein
Crystal structure of mtmc in complex with SAM
4RVD · D-mycarose 3-C-methyltransferase: “Crystal structure of mtmc in complex with SAM”. X-ray diffraction, 2 ligands (SAM, ZN), 1 pocket (best druggability 0.84). MolNFT v1 #106308 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4RVD
- Type
- protein
- Length
- 418 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-mycarose 3-C-methyltransferase
- UniProt
- Q194Q4
- Ligands
- SAM, ZN
- Pockets
- 1 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-mycarose 3-C-methyltransferase | protein | 418 | 38% helix, 22% strand | Q194Q4 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · chains A
- ZN · Zinc ion · metal · chains A
- ACT · Acetate ion · additive · 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 | 1007 | 0.84 | 0.85 | 95 | SAM |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 4RVD · Crystal structure of MtmC in complex with SAM · 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 Q194Q4
- Elsewhere: RCSB PDB 4RVD · PDBe 4RVD · UniProt Q194Q4
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