Research workbench
C-terminal domain of escherichia COLI arginine repressor
Analyse C-terminal domain of escherichia COLI arginine repressor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XXC
- Type
- protein
- Length
- 432 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arginine repressor
- UniProt
- P0A6D0
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Arginine repressor | protein | 72 | 33% helix, 32% strand | P0A6D0 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1042 | 0.78 | 0.80 | 78 | empty |
| 2 | 53 | 0.32 | 0.78 | 14 | empty |
| 3 | 55 | 0.32 | 0.77 | 15 | empty |
Interfaces
9 interfaces between chains.
- D–F · 556 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 551 Ų buried · 5 hydrogen bonds · protein-protein
- D–E · 546 Ų buried · 3 hydrogen bonds · protein-protein
- E–F · 531 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 525 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
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 P0A6D0
- Elsewhere: RCSB PDB 1XXC · PDBe 1XXC · UniProt P0A6D0
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