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Crystal structure of accessory secretory protein 1,2 and 3 in streptococcus pneumoniae
Analyse Crystal structure of accessory secretory protein 1,2 and 3 in streptococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LNW
- Type
- protein
- Length
- 767 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Accessory secretory protein ASP1; Accessory secretory protein ASP2; Accessory secretory…
- UniProt
- A0A0H2UR88, A0A0H2URA6, A0A0H2URJ0
- Pockets
- 9 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 25% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Accessory secretory protein ASP1 | protein | 495 | 36% helix, 25% strand | A0A0H2UR88 |
| B | Accessory secretory protein ASP2 | protein | 129 | 5% helix, 64% strand | A0A0H2URA6 |
| C | Accessory secretory protein ASP3 | protein | 143 | 3% helix, 45% strand | A0A0H2URJ0 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 626 | 0.75 | 0.82 | 65 | empty |
| 2 | 424 | 0.73 | 0.83 | 62 | empty |
| 3 | 386 | 0.66 | 0.80 | 37 | empty |
| 4 | 99 | 0.59 | 0.87 | 21 | empty |
| 5 | 316 | 0.56 | 0.76 | 27 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1795 Ų buried · 27 hydrogen bonds · protein-protein
- A–B · 803 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 587 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 6LNW · Crystal structure of accessory secretory protein 1,2 and 3 in Streptococcus pneumoniae · 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 A0A0H2UR88
- Every structure of UniProt A0A0H2URA6
- Every structure of UniProt A0A0H2URJ0
- Elsewhere: RCSB PDB 6LNW · PDBe 6LNW · UniProt A0A0H2UR88 · UniProt A0A0H2URA6 · UniProt A0A0H2URJ0
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