Research workbench
PRMT5:MEP50 complexed with adenosine
Analyse PRMT5:MEP50 complexed with adenosine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MXC
- Type
- protein
- Length
- 919 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein arginine N-methyltransferase 5; Methylosome protein 50
- EC
- 2.1.1.320
- UniProt
- O14744, Q9BQA1
- Ligands
- ADN
- Pockets
- 10 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein arginine N-methyltransferase 5 (EC 2.1.1.320) | protein | 621 | 31% helix, 27% strand | O14744 |
| B | Methylosome protein 50 | protein | 298 | 0% helix, 51% strand | Q9BQA1 |
Ligands and binding sites
- ADN · Adenosine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 611 | 0.84 | 0.89 | 58 | empty |
| 2 | 425 | 0.81 | 0.89 | 43 | empty |
| 3 | 173 | 0.81 | 0.96 | 29 | ADN |
| 4 | 407 | 0.59 | 0.75 | 41 | empty |
| 5 | 180 | 0.57 | 0.80 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2163 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 7MXC · PRMT5:MEP50 complexed with adenosine · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BQA1 · AlphaFold monomer V2.0 prediction for methylosome protein 50 (Q9BQA1) · a predicted model of the same protein · chain B against A, TM-score 1.00
- O14744 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 5 (O14744) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O14744
- Every structure of UniProt Q9BQA1
- Elsewhere: RCSB PDB 7MXC · PDBe 7MXC · UniProt O14744 · UniProt Q9BQA1
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