Research workbench
Crystal structure of the hybrid C-terminal domain of enzyme I of the bacterial phosphotransferase system formed by hybridizing the scaffold of the escherichia COLI enzyme with the active site loops from the thermoanaerobacter tengcongensis enzyme
Analyse Crystal structure of the hybrid C-terminal domain of enzyme I of the bacterial… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V9K
- Type
- protein
- Length
- 620 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoenolpyruvate-protein phosphotransferase
- EC
- 2.7.3.9
- UniProt
- A0A4S4CN20
- Ligands
- MG
- Pockets
- 5 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphoenolpyruvate-protein phosphotransferase (EC 2.7.3.9) | protein | 310 | 51% helix, 13% strand | A0A4S4CN20 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.55 | 0.76 | 37 | empty |
| 2 | 234 | 0.54 | 0.77 | 31 | empty |
| 3 | 115 | 0.38 | 0.74 | 29 | empty |
| 4 | 83 | 0.37 | 0.76 | 13 | empty |
| 5 | 69 | 0.35 | 0.77 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 1990 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 6V9K · Crystal structure of the hybrid C-terminal domain of enzyme I of the bacterial… · 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 A0A4S4CN20
- Elsewhere: RCSB PDB 6V9K · PDBe 6V9K · UniProt A0A4S4CN20
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