Research workbench
X-ray structure of psaa from yersinia pestis, in complex with galactose
Analyse X-ray structure of psaa from yersinia pestis, in complex with galactose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F8P
- Type
- protein
- Length
- 283 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PH 6 antigen
- UniProt
- P31522
- Ligands
- TBF, GAL
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PH 6 antigen | protein | 141 | 2% helix, 57% strand | P31522 |
| B | PH 6 antigen | protein | 142 | 4% helix, 55% strand | P31522 |
Ligands and binding sites
- TBF · Tert-butyl formate · ligand · chains A, B
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
- ACT · Acetate ion · additive · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.51 | 0.83 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 505 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
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 P31522
- Elsewhere: RCSB PDB 4F8P · PDBe 4F8P · UniProt P31522
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