Research workbench
Crystal structure of a tetr family transcription regulator (MAQU_1417) from marinobacter aquaeolei VT8 at 1.90 a resolution
Analyse Crystal structure of a tetr family transcription regulator (MAQU_1417) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PAS
- Type
- protein
- Length
- 767 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetr family transcription regulator
- UniProt
- A1U0I5
- Pockets
- 7 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 78% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetr family transcription regulator | protein | 191 | 80% helix, 1% strand | A1U0I5 |
| B | Tetr family transcription regulator | protein | 192 | 76% helix, 1% strand | A1U0I5 |
| C, D | Tetr family transcription regulator | protein | 192 | 77% helix, 1% strand | A1U0I5 |
Ligands and binding sites
- ACT · Acetate ion · additive · 12 copies · chains A, B, C, D
- PGO · S-1,2-propanediol · additive · 5 copies · chains A, D, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1026 | 0.85 | 0.86 | 78 | ACT |
| 2 | 1172 | 0.85 | 0.86 | 97 | ACT |
| 3 | 408 | 0.84 | 0.92 | 36 | ACT |
| 4 | 611 | 0.81 | 0.86 | 37 | empty |
| 5 | 74 | 0.48 | 0.83 | 19 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1325 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 1247 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 469 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 409 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 206 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 15 modified (engineered).
Compared structures
- 3PAS · Crystal structure of a TetR family transcription regulator (Maqu_1417) from MARINOBACTER… · 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 A1U0I5
- Elsewhere: RCSB PDB 3PAS · PDBe 3PAS · UniProt A1U0I5
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