Research workbench
Crystal structure of the ccpe regulatory domain at 1.95 ångström from staphylococcus aureus
Analyse Crystal structure of the ccpe regulatory domain at 1.95 ångström from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Y9Q
- Type
- protein
- Length
- 392 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbon catabolite responsive regulator
- UniProt
- A0A122PQF6
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Carbon catabolite responsive regulator | protein | 196 | 37% helix, 32% strand | A0A122PQF6 |
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 | 292 | 0.67 | 0.82 | 49 | empty |
| 2 | 266 | 0.59 | 0.79 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1403 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 5Y9Q · Crystal structure of the CcpE regulatory domain at 1.95 Angstrom from Staphylococcus… · 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 A0A122PQF6
- Elsewhere: RCSB PDB 5Y9Q · PDBe 5Y9Q · UniProt A0A122PQF6
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