Research workbench
Crystal structure of C.ELEGANS PRMT7 in complex with SAH(P31)
Analyse Crystal structure of C.ELEGANS PRMT7 in complex with SAH(P31) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WST
- Type
- protein
- Length
- 11,495 residues
- Chains
- 18
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein arginine N-methyltransferase 7
- EC
- 2.1.1.-
- UniProt
- Q9XW42
- Ligands
- SAH, PO4
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 9 distinct chains · 26% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, O, K | Protein arginine N-methyltransferase 7 (EC 2.1.1.-) | protein | 641 | 26% helix, 30% strand | Q9XW42 |
| D | Protein arginine N-methyltransferase 7 (EC 2.1.1.-) | protein | 637 | 26% helix, 30% strand | Q9XW42 |
| B, F, N, R | Protein arginine N-methyltransferase 7 (EC 2.1.1.-) | protein | 638 | 25% helix, 30% strand | Q9XW42 |
| C, H | Protein arginine N-methyltransferase 7 (EC 2.1.1.-) | protein | 639 | 27% helix, 30% strand | Q9XW42 |
| E, P | Protein arginine N-methyltransferase 7 (EC 2.1.1.-) | protein | 636 | 25% helix, 30% strand | Q9XW42 |
| G | Protein arginine N-methyltransferase 7 (EC 2.1.1.-) | protein | 636 | 25% helix, 30% strand | Q9XW42 |
| I, J, L | Protein arginine N-methyltransferase 7 (EC 2.1.1.-) | protein | 644 | 25% helix, 30% strand | Q9XW42 |
| M | Protein arginine N-methyltransferase 7 (EC 2.1.1.-) | protein | 633 | 27% helix, 30% strand | Q9XW42 |
| Q | Protein arginine N-methyltransferase 7 (EC 2.1.1.-) | protein | 632 | 26% helix, 28% strand | Q9XW42 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 18 copies · chains A, D, B, C, F, E, G, H, I, M, N, O, P, Q, R, J, K, L
- PO4 · Phosphate ion · ion · 18 copies · chains A, D, B, C, F, E, G, H, I, M, N, O, P, Q, R, J, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1120 | 0.83 | 0.84 | 128 | SAH |
| 2 | 1061 | 0.82 | 0.83 | 114 | SAH |
| 3 | 1045 | 0.81 | 0.83 | 117 | SAH |
| 4 | 940 | 0.81 | 0.82 | 107 | SAH |
| 5 | 889 | 0.80 | 0.82 | 95 | empty |
Interfaces
40 interfaces between chains.
- P–R · 843 Ų buried · 6 hydrogen bonds · protein-protein
- N–O · 842 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 823 Ų buried · 4 hydrogen bonds · protein-protein
- F–E · 821 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 812 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3WST · Crystal structure of C.elegans PRMT7 in complex with SAH(P31) · the same entry in another collection · chain H against H, 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 Q9XW42
- Elsewhere: RCSB PDB 3WST · PDBe 3WST · UniProt Q9XW42
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.