Research workbench
Crystal structure of shrimp alkaline phosphatase
Analyse Crystal structure of shrimp alkaline phosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K7H
- Type
- protein
- Length
- 952 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alkaline phosphatase
- EC
- 3.1.3.1
- UniProt
- Q9BHT8
- Ligands
- MAE, NAG, ZN, SO4
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alkaline phosphatase (EC 3.1.3.1) | protein | 476 | 34% helix, 19% strand | Q9BHT8 |
Ligands and binding sites
- MAE · Maleic acid · ligand · 3 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
- ZN · Zinc ion · metal · 6 copies · chains A, B
- SO4 · Sulfate ion · ion · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.79 | 0.98 | 29 | MAE |
| 2 | 92 | 0.44 | 0.79 | 23 | empty |
| 3 | 57 | 0.41 | 0.82 | 18 | empty |
| 4 | 83 | 0.40 | 0.78 | 22 | empty |
| 5 | 85 | 0.40 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 505 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 1K7H · Crystal structure of shrimp alkaline phosphatase · 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 Q9BHT8
- Elsewhere: RCSB PDB 1K7H · PDBe 1K7H · UniProt Q9BHT8
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