Research workbench
NMR data driven structural model of G-domain of mnme protein
Analyse NMR data driven structural model of G-domain of mnme protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RFL
- Type
- protein
- Length
- 172 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable tRNA modification GTPase trme
- UniProt
- P25522
- Pockets
- 4 · best druggability 0.65
Structure
solution nmr · 1 distinct chain · 23% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable tRNA modification GTPase trme | protein | 172 | 23% helix, 8% strand | P25522 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 180 | 0.65 | 0.85 | 36 | empty |
| 2 | 110 | 0.62 | 0.87 | 21 | empty |
| 3 | 291 | 0.56 | 0.76 | 49 | empty |
| 4 | 79 | 0.41 | 0.79 | 16 | empty |
Compared structures
- 1RFL · NMR data driven structural model of G-domain of MnmE protein · the same entry in another collection · chain A against A, TM-score 1.00
- P25522 · AlphaFold monomer V2.0 prediction for tRNA modification GTPase mnme (P25522) · a predicted model of the same protein · chain A against A, TM-score 0.56
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 P25522
- Elsewhere: RCSB PDB 1RFL · PDBe 1RFL · UniProt P25522
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