Research workbench
Crystal structure of a putative TRP repressor from staphylococcus aureus
Analyse Crystal structure of a putative TRP repressor from staphylococcus aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KOR
- Type
- protein
- Length
- 401 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Possible TRP repressor
- UniProt
- A8Z2S1
- Pockets
- 7 · best druggability 0.64
Structure
x-ray diffraction · 3 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Possible TRP repressor | protein | 100 | 74% helix, 0% strand | A8Z2S1 |
| B | Possible TRP repressor | protein | 101 | 73% helix, 0% strand | A8Z2S1 |
| C | Possible TRP repressor | protein | 100 | 75% helix, 0% strand | A8Z2S1 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 601 | 0.64 | 0.75 | 44 | empty |
| 2 | 114 | 0.41 | 0.76 | 21 | empty |
| 3 | 114 | 0.39 | 0.75 | 17 | empty |
| 4 | 98 | 0.37 | 0.76 | 21 | empty |
| 5 | 80 | 0.35 | 0.76 | 21 | empty |
Interfaces
6 interfaces between chains.
- B–C · 2916 Ų buried · 48 hydrogen bonds · protein-protein
- A–D · 2906 Ų buried · 48 hydrogen bonds · protein-protein
- A–C · 100 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 76 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 72 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 3KOR · Crystal structure of a putative Trp repressor from Staphylococcus aureus · 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 A8Z2S1
- Elsewhere: RCSB PDB 3KOR · PDBe 3KOR · UniProt A8Z2S1
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