Research workbench
Conformation of methylated ggq in the peptidyl transferase center during translation termination (ptc region)
Analyse Conformation of methylated ggq in the peptidyl transferase center during… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C4H
- Type
- protein + RNA
- Length
- 832 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 23S rRNA; 50S ribosomal protein L2; 50S ribosomal protein L3; 50S ribosomal protein L16…
- UniProt
- P60422, P60438, P0ADY7, P0A7L8, P07012
- Ligands
- MG
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 7 distinct chains · 13% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 23S rRNA | rna | 636 | — | — |
| C | 50S ribosomal protein L2 | protein | 47 | 6% helix, 4% strand | P60422 |
| D | 50S ribosomal protein L3 | protein | 47 | 9% helix, 0% strand | P60438 |
| N | 50S ribosomal protein L16 | protein | 17 | 0% helix, 12% strand | P0ADY7 |
| X | 50S ribosomal protein L27 | protein | 10 | 0% helix, 0% strand | P0A7L8 |
| x | P-site tRNA fmet | rna | 12 | — | — |
| v | Peptide chain release factor RF2 | protein | 63 | 25% helix, 27% strand | P07012 |
Ligands and binding sites
- MG · Magnesium ion · metal · 34 copies · chains A, C
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 | 638 | 0.85 | 0.90 | 69 | MG |
| 2 | 1185 | 0.84 | 0.86 | 83 | MG |
| 3 | 630 | 0.84 | 0.90 | 59 | MG |
| 4 | 674 | 0.82 | 0.87 | 77 | MG |
| 5 | 854 | 0.81 | 0.85 | 59 | MG |
Interfaces
11 interfaces between chains.
- A–C · 2519 Ų buried · 58 hydrogen bonds · protein-nucleic
- A–D · 2269 Ų buried · 66 hydrogen bonds · protein-nucleic
- A–v · 1422 Ų buried · 35 hydrogen bonds · protein-nucleic
- A–N · 760 Ų buried · 17 hydrogen bonds · protein-nucleic
- A–X · 608 Ų buried · 14 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 18 modified (nucleotide modification, nonstandard).
Compared structures
- 6C4H · Conformation of methylated GGQ in the peptidyl transferase center during translation… · the same entry in another collection · chain v against v, TM-score 1.00
- P07012 · AlphaFold monomer V2.0 prediction for peptide chain release factor RF2 (P07012) · a predicted model of the same protein · chain v against A, TM-score 0.91
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 P60422
- Every structure of UniProt P60438
- Every structure of UniProt P0ADY7
- Every structure of UniProt P0A7L8
- Every structure of UniProt P07012
- Elsewhere: RCSB PDB 6C4H · PDBe 6C4H · UniProt P60422 · UniProt P60438 · UniProt P0ADY7 · UniProt P0A7L8 · UniProt P07012
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