Research workbench
Structure of the ATPase subunit cysa of the putative sulfate ATP- binding cassette (ABC) transporter from alicyclobacillus acidocaldarius
Analyse Structure of the ATPase subunit cysa of the putative sulfate ATP- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z47
- Type
- protein
- Length
- 687 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative ABC-transporter ATP-binding protein
- UniProt
- Q9RHZ7
- Ligands
- CL
- Pockets
- 6 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative ABC-transporter ATP-binding protein | protein | 345 | 30% helix, 33% strand | Q9RHZ7 |
| B | Putative ABC-transporter ATP-binding protein | protein | 342 | 28% helix, 33% strand | Q9RHZ7 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 176 | 0.56 | 0.80 | 18 | empty |
| 2 | 207 | 0.50 | 0.76 | 29 | empty |
| 3 | 200 | 0.48 | 0.75 | 18 | empty |
| 4 | 211 | 0.47 | 0.75 | 28 | empty |
| 5 | 64 | 0.34 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 331 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1Z47 · Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC)… · 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 Q9RHZ7
- Elsewhere: RCSB PDB 1Z47 · PDBe 1Z47 · UniProt Q9RHZ7
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