Research workbench
Structure of complex between E. COLI translation termination factor RF1 and the prmc methyltransferase
Analyse Structure of complex between E. COLI translation termination factor RF1 and the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B3T
- Type
- protein
- Length
- 576 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein methyltransferase hemk; Peptide chain release factor 1
- EC
- 2.1.1.-
- UniProt
- P37186, P0A7I0
- Ligands
- SAH
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein methyltransferase hemk (EC 2.1.1.-) | protein | 276 | 43% helix, 19% strand | P37186 |
| B | Peptide chain release factor 1 | protein | 300 | 36% helix, 23% strand | P0A7I0 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.74 | 0.93 | 33 | SAH |
| 2 | 232 | 0.54 | 0.77 | 25 | empty |
| 3 | 187 | 0.52 | 0.78 | 31 | empty |
| 4 | 254 | 0.49 | 0.74 | 24 | empty |
| 5 | 116 | 0.43 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1845 Ų buried · 36 hydrogen bonds · protein-protein
Compared structures
- 2B3T · Structure of complex between E. coli translation termination factor RF1 and the PrmC… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A7I0 · AlphaFold monomer V2.0 prediction for peptide chain release factor RF1 (P0A7I0) · a predicted model of the same protein · chain B against A, TM-score 0.70
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 P37186
- Every structure of UniProt P0A7I0
- Elsewhere: RCSB PDB 2B3T · PDBe 2B3T · UniProt P37186 · UniProt P0A7I0
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