Research workbench
Crystal structure of a mutant of acid phosphatase from escherichia blattae (G74D/I153T)
Analyse Crystal structure of a mutant of acid phosphatase from escherichia blattae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IW8
- Type
- protein
- Length
- 1,298 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acid phosphatase
- EC
- 3.1.3.2
- UniProt
- Q9S1A6
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 6 distinct chains · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acid phosphatase (EC 3.1.3.2) | protein | 217 | 65% helix, 0% strand | Q9S1A6 |
| B | Acid phosphatase (EC 3.1.3.2) | protein | 219 | 64% helix, 0% strand | Q9S1A6 |
| C | Acid phosphatase (EC 3.1.3.2) | protein | 216 | 66% helix, 0% strand | Q9S1A6 |
| D | Acid phosphatase (EC 3.1.3.2) | protein | 215 | 66% helix, 0% strand | Q9S1A6 |
| E | Acid phosphatase (EC 3.1.3.2) | protein | 214 | 66% helix, 0% strand | Q9S1A6 |
| F | Acid phosphatase (EC 3.1.3.2) | protein | 217 | 65% helix, 0% strand | Q9S1A6 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 711 | 0.77 | 0.82 | 73 | empty |
| 2 | 723 | 0.77 | 0.82 | 71 | empty |
| 3 | 693 | 0.77 | 0.82 | 69 | empty |
| 4 | 499 | 0.75 | 0.83 | 43 | empty |
| 5 | 463 | 0.73 | 0.82 | 45 | empty |
Interfaces
12 interfaces between chains.
- E–F · 1302 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 1300 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1285 Ų buried · 8 hydrogen bonds · protein-protein
- C–E · 280 Ų buried · 3 hydrogen bonds · protein-protein
- B–F · 278 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1IW8 · Crystal Structure of a mutant of acid phosphatase from Escherichia blattae (G74D/I153T) · 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 Q9S1A6
- Elsewhere: RCSB PDB 1IW8 · PDBe 1IW8 · UniProt Q9S1A6
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