Research workbench
Three-dimensional structure of the D153G mutant of E. COLI alkaline phosphatase: a mutant with weaker magnesium binding and increased catalytic activity
Analyse Three-dimensional structure of the D153G mutant of E. COLI alkaline… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AJA
- Type
- protein
- Length
- 869 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alkaline phosphatase
- EC
- 3.1.3.1
- UniProt
- P00634
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alkaline phosphatase (EC 3.1.3.1) | protein | 435 | 32% helix, 21% strand | P00634 |
| B | Alkaline phosphatase (EC 3.1.3.1) | protein | 434 | 33% helix, 22% strand | P00634 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 106 | 0.79 | 0.99 | 27 | empty |
| 2 | 673 | 0.70 | 0.78 | 92 | empty |
| 3 | 54 | 0.53 | 0.88 | 14 | empty |
| 4 | 55 | 0.50 | 0.87 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 3429 Ų buried · 58 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1AJA · Three-dimensional structure of the D153G mutant of E. COLI alkaline phosphatase: a mutant… · the same entry in another collection · chain A against A, TM-score 1.00
- P00634 · AlphaFold monomer V2.0 prediction for alkaline phosphatase (P00634) · a predicted model of the same protein · 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 P00634
- Elsewhere: RCSB PDB 1AJA · PDBe 1AJA · UniProt P00634
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