Research workbench
Phosphate-binding protein from stenotrophomonas maltophilia.
Analyse Phosphate-binding protein from stenotrophomonas maltophilia. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JK4
- Type
- protein
- Length
- 373 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alkaline phosphatase
- EC
- 3.1.3.1
- UniProt
- B4SL31
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alkaline phosphatase (EC 3.1.3.1) | protein | 373 | 31% helix, 19% strand | B4SL31 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.39 | 0.81 | 19 | empty |
| 2 | 61 | 0.36 | 0.78 | 18 | empty |
| 3 | 50 | 0.25 | 0.73 | 16 | empty |
Modifications
Observed in the structure: 2 disulfide, 1 modified (disulfide, cyclization).
Compared structures
- 5JK4 · Phosphate-Binding Protein from Stenotrophomonas maltophilia. · 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 B4SL31
- Elsewhere: RCSB PDB 5JK4 · PDBe 5JK4 · UniProt B4SL31
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.