Research workbench
Crystal structure of phosphotransferase system component eiia from streptococcus agalactiae
Analyse Crystal structure of phosphotransferase system component eiia from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4TKZ
- Type
- protein
- Length
- 780 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein GBS1890
- EC
- 2.7.1.69
- UniProt
- Q8E371
- Pockets
- 8 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Putative uncharacterized protein GBS1890 (EC 2.7.1.69) | protein | 130 | 48% helix, 21% strand | Q8E371 |
Ligands and binding sites
- GOL · Glycerol · additive · 11 copies · chains A, B, F, C, E, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.67 | 0.86 | 23 | GOL |
| 2 | 149 | 0.53 | 0.80 | 14 | GOL |
| 3 | 147 | 0.51 | 0.79 | 16 | empty |
| 4 | 246 | 0.49 | 0.74 | 34 | empty |
| 5 | 143 | 0.47 | 0.77 | 15 | GOL |
Interfaces
6 interfaces between chains.
- A–B · 1578 Ų buried · 24 hydrogen bonds · protein-protein
- D–F · 489 Ų buried · 6 hydrogen bonds · protein-protein
- B–F · 473 Ų buried · 7 hydrogen bonds · protein-protein
- C–E · 458 Ų buried · 4 hydrogen bonds · protein-protein
- A–E · 436 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4TKZ · Crystal structure of phosphotransferase system component EIIA from Streptococcus… · 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 Q8E371
- Elsewhere: RCSB PDB 4TKZ · PDBe 4TKZ · UniProt Q8E371
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