Research workbench
Apo form of comr from S. thermophilus in space group C2
Analyse Apo form of comr from S. thermophilus in space group C2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QER
- Type
- protein
- Length
- 1,199 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator
- UniProt
- A0A1L1QK15
- Pockets
- 16 · best druggability 0.83
Structure
x-ray diffraction · 3 distinct chains · 71% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transcriptional regulator | protein | 300 | 71% helix, 1% strand | A0A1L1QK15 |
| C | Transcriptional regulator | protein | 305 | 71% helix, 1% strand | A0A1L1QK15 |
| D | Transcriptional regulator | protein | 294 | 72% helix, 1% strand | A0A1L1QK15 |
Pockets
16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 796 | 0.83 | 0.86 | 95 | empty |
| 2 | 707 | 0.77 | 0.82 | 49 | empty |
| 3 | 563 | 0.76 | 0.82 | 42 | empty |
| 4 | 652 | 0.74 | 0.80 | 46 | empty |
| 5 | 564 | 0.64 | 0.75 | 54 | empty |
Interfaces
5 interfaces between chains.
- A–B · 932 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 526 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 287 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 134 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 84 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6QER · Apo Form Of ComR From S. Thermophilus in space group C2 · 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 A0A1L1QK15
- Elsewhere: RCSB PDB 6QER · PDBe 6QER · UniProt A0A1L1QK15
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