Research workbench
Structure of the qbeta holoenzyme complex in the P1211 crystal form
Analyse Structure of the qbeta holoenzyme complex in the P1211 crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4R71
- Type
- protein
- Length
- 2,725 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor ts, elongation factor tu; RNA-directed RNA polymerase beta chain; 30S…
- EC
- 2.7.7.48
- UniProt
- P0A6P1, P0CE48, P14647, P0AG67
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 6 distinct chains · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor ts, elongation factor tu | protein | 650 | 35% helix, 30% strand | P0A6P1, P0CE48 |
| B | RNA-directed RNA polymerase beta chain (EC 2.7.7.48) | protein | 556 | 45% helix, 16% strand | P14647 |
| C | Elongation factor ts, elongation factor tu | protein | 650 | 36% helix, 30% strand | P0A6P1, P0CE48 |
| D | RNA-directed RNA polymerase beta chain (EC 2.7.7.48) | protein | 553 | 43% helix, 17% strand | P14647 |
| E | 30S ribosomal protein S1 | protein | 157 | 18% helix, 35% strand | P0AG67 |
| F | 30S ribosomal protein S1 | protein | 159 | 18% helix, 36% strand | P0AG67 |
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 962 | 0.77 | 0.79 | 99 | empty |
| 2 | 1193 | 0.76 | 0.78 | 136 | empty |
| 3 | 771 | 0.70 | 0.76 | 76 | empty |
| 4 | 780 | 0.68 | 0.75 | 71 | empty |
| 5 | 739 | 0.68 | 0.76 | 70 | empty |
Interfaces
8 interfaces between chains.
- C–D · 2584 Ų buried · 27 hydrogen bonds · protein-protein
- A–B · 2515 Ų buried · 28 hydrogen bonds · protein-protein
- D–F · 2096 Ų buried · 34 hydrogen bonds · protein-protein
- B–E · 2064 Ų buried · 28 hydrogen bonds · protein-protein
- A–C · 303 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4R71 · Structure of the Qbeta holoenzyme complex in the P1211 crystal form · the same entry in another collection · chain F against F, TM-score 1.00
- P0AG67 · AlphaFold monomer V2.0 prediction for 30S ribosomal protein S1 (P0AG67) · a predicted model of the same protein · chain F against A, TM-score 0.48
- P0A6P1 · AlphaFold monomer V2.0 prediction for elongation factor ts (P0A6P1) · a predicted model of the same protein · chain C against A, TM-score 0.42
- P0CE48 · AlphaFold monomer V2.0 prediction for elongation factor tu 2 (P0CE48) · a predicted model of the same protein · chain A against A, TM-score 0.32
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 P0A6P1
- Every structure of UniProt P0CE48
- Every structure of UniProt P14647
- Every structure of UniProt P0AG67
- Elsewhere: RCSB PDB 4R71 · PDBe 4R71 · UniProt P0A6P1 · UniProt P0CE48 · UniProt P14647 · UniProt P0AG67
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