Research workbench
Crystal structure of the adhesin domain of epf from streptococcus pyogenes in P21
Analyse Crystal structure of the adhesin domain of epf from streptococcus pyogenes in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ES9
- Type
- protein
- Length
- 1,196 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epf
- Pockets
- 8 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 5% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epf | protein | 296 | 5% helix, 47% strand | — |
| B | Epf | protein | 300 | 5% helix, 47% strand | — |
| C | Epf | protein | 301 | 5% helix, 47% strand | — |
| D | Epf | protein | 299 | 5% helix, 47% strand | — |
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1093 | 0.85 | 0.86 | 119 | empty |
| 2 | 823 | 0.74 | 0.78 | 59 | empty |
| 3 | 854 | 0.70 | 0.75 | 73 | empty |
| 4 | 192 | 0.57 | 0.80 | 35 | empty |
| 5 | 158 | 0.49 | 0.77 | 19 | empty |
Interfaces
5 interfaces between chains.
- A–B · 674 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 590 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 437 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 320 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 217 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4ES9 · Crystal Structure of the adhesin domain of Epf from Streptococcus pyogenes in P21 · 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
- Elsewhere: RCSB PDB 4ES9 · PDBe 4ES9
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