Research workbench
Crystal structure francisella tularensis histidine acid phosphatase complexed with L(+)-tartrate
Analyse Crystal structure francisella tularensis histidine acid phosphatase complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IT1
- Type
- protein
- Length
- 657 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acid phosphatase
- EC
- 3.1.3.2
- UniProt
- Q2A612
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acid phosphatase (EC 3.1.3.2) | protein | 328 | 46% helix, 15% strand | Q2A612 |
| B | Acid phosphatase (EC 3.1.3.2) | protein | 329 | 46% helix, 16% strand | Q2A612 |
Ligands and binding sites
- PG0 · 2-(2-methoxyethoxy)ethanol · additive · 4 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
- TLA · L(+)-tartaric acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 341 | 0.67 | 0.81 | 39 | TLA |
| 2 | 346 | 0.67 | 0.81 | 41 | TLA |
| 3 | 50 | 0.28 | 0.76 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 1730 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 3IT1 · Crystal Structure Francisella tularensis histidine acid phosphatase complexed with… · 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 Q2A612
- Elsewhere: RCSB PDB 3IT1 · PDBe 3IT1 · UniProt Q2A612
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.