Research workbench
Human methyltransferase-like 18
Analyse Human methyltransferase-like 18 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RFQ
- Type
- protein
- Length
- 270 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine protein methyltransferase 1 homolog
- EC
- 2.1.1.-
- UniProt
- O95568
- Ligands
- SAM, UNX
- Pockets
- 2 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine protein methyltransferase 1 homolog (EC 2.1.1.-) | protein | 270 | 30% helix, 28% strand | O95568 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · chains A
- UNX · Unknown atom or ion · ion · 12 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.81 | 0.96 | 32 | SAM |
| 2 | 68 | 0.33 | 0.75 | 21 | empty |
Compared structures
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 O95568
- Elsewhere: RCSB PDB 4RFQ · PDBe 4RFQ · UniProt O95568
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