Research workbench
Crystal structure of staphylococcal enterotoxin G (seg) in complex with a high affinity mutant mouse T-cell receptor chain
Analyse Crystal structure of staphylococcal enterotoxin G (seg) in complex with a high… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OWE
- Type
- protein
- Length
- 2,691 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-chain; Enterotoxin seg
- UniProt
- A2NTY6, D0EMB6
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 17% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K, M, O | Beta-chain | protein | 109 | 3% helix, 57% strand | A2NTY6 |
| B, D, F, H, J | Enterotoxin seg | protein | 227 | 21% helix, 35% strand | D0EMB6 |
| L, N, P | Enterotoxin seg | protein | 228 | 21% helix, 36% strand | D0EMB6 |
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1027 | 0.82 | 0.83 | 120 | empty |
| 2 | 1154 | 0.82 | 0.83 | 123 | empty |
| 3 | 593 | 0.78 | 0.84 | 64 | empty |
| 4 | 584 | 0.78 | 0.84 | 65 | empty |
| 5 | 402 | 0.76 | 0.86 | 53 | empty |
Interfaces
35 interfaces between chains.
- F–J · 742 Ų buried · 2 hydrogen bonds · protein-protein
- B–N · 718 Ų buried · 3 hydrogen bonds · protein-protein
- H–L · 707 Ų buried · 4 hydrogen bonds · protein-protein
- D–P · 689 Ų buried · 4 hydrogen bonds · protein-protein
- K–L · 683 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide (disulfide).
Compared structures
- 3OWE · Crystal Structure of Staphylococcal Enterotoxin G (SEG) in Complex with a High Affinity… · 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 A2NTY6
- Every structure of UniProt D0EMB6
- Elsewhere: RCSB PDB 3OWE · PDBe 3OWE · UniProt A2NTY6 · UniProt D0EMB6
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