Research workbench
In situ structure of capping enzyme LAMBDA2, penetration protein MU1 of mammalian reovirus capsid asymmetric unit.
Analyse In situ structure of capping enzyme LAMBDA2, penetration protein MU1 of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ELL
- Type
- protein
- Length
- 7,917 residues
- Chains
- 21
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MU1; MRNA (guanine-N(7)-)-methyltransferase
- EC
- 2.1.1.56, 2.7.7.50
- UniProt
- F1ARM5, A0A0B5CUT9
- Ligands
- MYR
- Pockets
- 20 · best druggability 0.89
Structure
electron microscopy · 7 distinct chains · 31% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MU1 | protein | 41 | 17% helix, 12% strand | F1ARM5 |
| a | MU1 | protein | 610 | 37% helix, 19% strand | F1ARM5 |
| B, C, D, E, F, G, H, J | MU1 | protein | 33 | 18% helix, 12% strand | F1ARM5 |
| b, c, d, e, f, g, i, j | MU1 | protein | 633 | 36% helix, 19% strand | F1ARM5 |
| h | MU1 | protein | 623 | 37% helix, 18% strand | F1ARM5 |
| I | MU1 | protein | 32 | 22% helix, 9% strand | F1ARM5 |
| K | MRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.56, 2.7.7.50) | protein | 1283 | 24% helix, 24% strand | A0A0B5CUT9 |
Ligands and binding sites
- MYR · Myristic acid · ligand · 10 copies · chains A, a, K, B, b, C, c, d, E, e, F, f, G, g, h, I, i, J, j
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 | 1083 | 0.89 | 0.90 | 133 | empty |
| 2 | 1054 | 0.88 | 0.90 | 123 | empty |
| 3 | 1080 | 0.88 | 0.89 | 114 | empty |
| 4 | 821 | 0.85 | 0.87 | 89 | empty |
| 5 | 861 | 0.84 | 0.86 | 97 | empty |
Interfaces
67 interfaces between chains.
- d–f · 4681 Ų buried · 36 hydrogen bonds · protein-protein
- a–b · 4642 Ų buried · 39 hydrogen bonds · protein-protein
- d–e · 4605 Ų buried · 44 hydrogen bonds · protein-protein
- g–h · 4603 Ų buried · 44 hydrogen bonds · protein-protein
- g–i · 4561 Ų buried · 39 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 lipid (myristoylation).
Compared structures
- 7ELL · In situ structure of capping enzyme lambda2, penetration protein mu1 of mammalian… · 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 F1ARM5
- Every structure of UniProt A0A0B5CUT9
- Elsewhere: RCSB PDB 7ELL · PDBe 7ELL · UniProt F1ARM5 · UniProt A0A0B5CUT9
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