Research workbench
Crystal structure of P. aeruginosa tpba
Analyse Crystal structure of P. aeruginosa tpba in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4R0S
- Type
- protein
- Length
- 323 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein tyrosine phosphatase tpba
- UniProt
- Q9HXC7
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein tyrosine phosphatase tpba | protein | 162 | 49% helix, 15% strand | Q9HXC7 |
| B | Protein tyrosine phosphatase tpba | protein | 161 | 50% helix, 16% strand | Q9HXC7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.46 | 0.81 | 12 | empty |
| 2 | 114 | 0.42 | 0.77 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 384 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4R0S · Crystal structure of P. aeruginosa TpbA · 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 Q9HXC7
- Elsewhere: RCSB PDB 4R0S · PDBe 4R0S · UniProt Q9HXC7
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