Research workbench
Crystal structure of a tetr family transcriptional regulator pfmr from thermus thermophilus HB8
Analyse Crystal structure of a tetr family transcriptional regulator pfmr from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VPR
- Type
- protein
- Length
- 743 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator, tetr family
- UniProt
- Q53WD9
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 77% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator, tetr family | protein | 189 | 77% helix, 1% strand | Q53WD9 |
| B | Transcriptional regulator, tetr family | protein | 187 | 75% helix, 1% strand | Q53WD9 |
| C | Transcriptional regulator, tetr family | protein | 182 | 79% helix, 1% strand | Q53WD9 |
| D | Transcriptional regulator, tetr family | protein | 185 | 78% helix, 1% strand | Q53WD9 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1173 | 0.79 | 0.80 | 87 | empty |
| 2 | 911 | 0.76 | 0.79 | 75 | empty |
Interfaces
4 interfaces between chains.
- C–D · 1836 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 1737 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 355 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 126 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 20 modified (engineered).
Compared structures
- 3VPR · Crystal Structure of a TetR Family Transcriptional Regulator PfmR from Thermus… · 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 Q53WD9
- Elsewhere: RCSB PDB 3VPR · PDBe 3VPR · UniProt Q53WD9
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