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Structural characteristics of alkaline phosphatase from a moderately halophilic bacteria halomonas SP.593
Analyse Structural characteristics of alkaline phosphatase from a moderately halophilic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WBH
- Type
- protein
- Length
- 994 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alkaline phosphatase
- EC
- 3.1.3.1
- UniProt
- B5BP20
- Ligands
- MG, ZN, CL
- Pockets
- 8 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alkaline phosphatase (EC 3.1.3.1) | protein | 497 | 41% helix, 17% strand | B5BP20 |
Ligands and binding sites
- MG · Magnesium ion · metal · 6 copies · chains A, B
- ZN · Zinc ion · metal · 4 copies · chains A, B
- CL · Chloride ion · ion · 2 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 325 | 0.59 | 0.77 | 38 | CL |
| 2 | 323 | 0.58 | 0.77 | 41 | CL |
| 3 | 127 | 0.43 | 0.76 | 17 | empty |
| 4 | 122 | 0.41 | 0.76 | 23 | empty |
| 5 | 106 | 0.39 | 0.76 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 4380 Ų buried · 63 hydrogen bonds · protein-protein
Compared structures
- 3WBH · Structural characteristics of alkaline phosphatase from a moderately halophilic bacteria… · 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 B5BP20
- Elsewhere: RCSB PDB 3WBH · PDBe 3WBH · UniProt B5BP20
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