Research workbench
DNA binding domain of the phage T4 transcription factor mota (AA105-211)
Analyse DNA binding domain of the phage T4 transcription factor mota (AA105-211) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KAF
- Type
- protein
- Length
- 635 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription regulatory protein mota
- UniProt
- P22915
- Pockets
- 7 · best druggability 0.63
Structure
x-ray diffraction · 3 distinct chains · 34% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Transcription regulatory protein mota | protein | 108 | 33% helix, 38% strand | P22915 |
| D, F | Transcription regulatory protein mota | protein | 104 | 35% helix, 39% strand | P22915 |
| E | Transcription regulatory protein mota | protein | 103 | 33% helix, 40% strand | P22915 |
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 | 563 | 0.63 | 0.75 | 54 | empty |
| 2 | 450 | 0.61 | 0.76 | 58 | empty |
| 3 | 335 | 0.53 | 0.74 | 32 | empty |
| 4 | 285 | 0.53 | 0.75 | 42 | empty |
| 5 | 147 | 0.39 | 0.73 | 21 | empty |
Interfaces
8 interfaces between chains.
- A–D · 362 Ų buried · 6 hydrogen bonds · protein-protein
- E–F · 322 Ų buried · 7 hydrogen bonds · protein-protein
- C–F · 307 Ų buried · 3 hydrogen bonds · protein-protein
- D–E · 295 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 282 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1KAF · DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211) · 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 P22915
- Elsewhere: RCSB PDB 1KAF · PDBe 1KAF · UniProt P22915
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