Research workbench
High affinity fucose binding of pseudomonas aeruginosa lectin II: 1.0 a crystal structure of the complex
Analyse High affinity fucose binding of pseudomonas aeruginosa lectin II: 1.0 a crystal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UZV
- Type
- protein
- Length
- 456 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pseudomonas aeruginosa lectin II
- UniProt
- Q9HYN5
- Ligands
- FUC, CA, SO4
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 71% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Pseudomonas aeruginosa lectin II | protein | 114 | 0% helix, 71% strand | Q9HYN5 |
Ligands and binding sites
- FUC · alpha-L-fucopyranose · sugar · 4 copies · chains A, B, C, D
- CA · Calcium ion · metal · 8 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.34 | 0.73 | 19 | empty |
| 2 | 73 | 0.28 | 0.72 | 19 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1327 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 1326 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 520 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 518 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 212 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1UZV · High affinity fucose binding of Pseudomonas aeruginosa lectin II: 1.0 A crystal structure… · 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 Q9HYN5
- Elsewhere: RCSB PDB 1UZV · PDBe 1UZV · UniProt Q9HYN5
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