Research workbench
Human HMT1 hnrnp methyltransferase-like protein 6 (S. cerevisiae)
Analyse Human HMT1 hnrnp methyltransferase-like protein 6 (S. cerevisiae) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WCF
- Type
- protein
- Length
- 319 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein arginine N-methyltransferase 6
- EC
- 2.1.1.319
- UniProt
- Q96LA8
- Ligands
- SAH, A0S
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein arginine N-methyltransferase 6 (EC 2.1.1.319) | protein | 319 | 32% helix, 36% strand | Q96LA8 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
- A0S · (5R)-4-(5-bromofuran-2-carbonyl)-5-(4-fluorophenyl)-7-methyl-1,3,4,5-tetrahydro-2H-1,4-benzodiazepin-2-one · ligand · chains A
- 144 · Tris-hydroxymethyl-methyl-ammonium · additive · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 216 | 0.82 | 0.94 | 32 | A0S |
| 2 | 328 | 0.60 | 0.77 | 37 | SAH, 144 |
Compared structures
- 5WCF · Human HMT1 hnRNP methyltransferase-like protein 6 (S. cerevisiae) · the same entry in another collection · chain A against A, TM-score 1.00
- Q96LA8 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 6 (Q96LA8) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q96LA8
- Elsewhere: RCSB PDB 5WCF · PDBe 5WCF · UniProt Q96LA8
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