Research workbench
X-ray structure of the sugar N-methyltransferase KEDS8 from streptoalloteichus sp atcc 53650
Analyse X-ray structure of the sugar N-methyltransferase KEDS8 from streptoalloteichus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5BSZ
- Type
- protein
- Length
- 247 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-methyltransferase
- UniProt
- K4P132
- Ligands
- SAH, THM
- Pockets
- 1 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-methyltransferase | protein | 247 | 27% helix, 31% strand | K4P132 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
- THM · Thymidine · ligand · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · 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 | 748 | 0.77 | 0.81 | 69 | SAH, THM |
Compared structures
- 5BSZ · X-ray structure of the sugar N-methyltransferase KedS8 from Streptoalloteichus sp ATCC… · 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 K4P132
- Elsewhere: RCSB PDB 5BSZ · PDBe 5BSZ · UniProt K4P132
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