Research workbench
Crystal structure of the hypothetical tandem-type universal stress protein TTHA0350 complexed with atps.
Analyse Crystal structure of the hypothetical tandem-type universal stress protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AB8
- Type
- protein
- Length
- 521 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein TTHA0350
- UniProt
- Q5SLE3
- Ligands
- ATP, MG
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative uncharacterized protein TTHA0350 | protein | 261 | 47% helix, 21% strand | Q5SLE3 |
| B | Putative uncharacterized protein TTHA0350 | protein | 260 | 47% helix, 22% strand | Q5SLE3 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, B
- MG · Magnesium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 620 | 0.76 | 0.82 | 41 | empty |
| 2 | 185 | 0.71 | 0.89 | 28 | ATP, MG |
| 3 | 175 | 0.71 | 0.89 | 28 | ATP, MG |
| 4 | 120 | 0.51 | 0.81 | 20 | ATP |
| 5 | 115 | 0.48 | 0.79 | 22 | ATP |
Interfaces
1 interface between chains.
- A–B · 910 Ų buried · 29 hydrogen bonds · protein-protein
Compared structures
- 3AB8 · Crystal Structure of the Hypothetical Tandem-type Universal Stress Protein TTHA0350… · 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 Q5SLE3
- Elsewhere: RCSB PDB 3AB8 · PDBe 3AB8 · UniProt Q5SLE3
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