MolNFT v1 · #106888 · protein
Structure of the C-terminal spoa domain of shigella flexneri SPA33
4TT9 · Surface presentation of antigens protein spao: “Structure of the C-terminal spoa domain of shigella flexneri SPA33”. X-ray diffraction. MolNFT v1 #106888 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4TT9
- Type
- protein
- Length
- 282 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Surface presentation of antigens protein spao
- UniProt
- P0A1K9
Structure
x-ray diffraction · 4 distinct chains · 10% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Surface presentation of antigens protein spao | protein | 70 | 13% helix, 60% strand | P0A1K9 |
| B | Surface presentation of antigens protein spao | protein | 72 | 7% helix, 56% strand | P0A1K9 |
| C | Surface presentation of antigens protein spao | protein | 72 | 13% helix, 51% strand | P0A1K9 |
| D | Surface presentation of antigens protein spao | protein | 68 | 6% helix, 59% strand | P0A1K9 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
6 interfaces between chains.
- A–B · 2284 Ų buried · 41 hydrogen bonds · protein-protein
- C–D · 2213 Ų buried · 46 hydrogen bonds · protein-protein
- B–D · 255 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 230 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 138 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 4TT9 · Structure of the C-terminal SpoA domain of Shigella flexneri Spa33 · the same entry in another collection · chain D against D, TM-score 1.00
- P0A1K9 · AlphaFold monomer V2.0 prediction for surface presentation of antigens protein spao… · a predicted model of the same protein · chain B against A, TM-score 0.86
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 P0A1K9
- Elsewhere: RCSB PDB 4TT9 · PDBe 4TT9 · UniProt P0A1K9
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