Research workbench
Structure of the staphylococcus aureus putative ATPase subunit of an ATP-binding cassette (ABC) transporter
Analyse Structure of the staphylococcus aureus putative ATPase subunit of an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IHY
- Type
- protein
- Length
- 509 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC transporter, ATP-binding protein
- EC
- 3.6.3.34
- UniProt
- Q5HE50
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ABC transporter, ATP-binding protein (EC 3.6.3.34) | protein | 248 | 35% helix, 31% strand | Q5HE50 |
| B | ABC transporter, ATP-binding protein (EC 3.6.3.34) | protein | 261 | 34% helix, 30% strand | Q5HE50 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.63 | 0.86 | 29 | empty |
| 2 | 108 | 0.45 | 0.78 | 17 | empty |
| 3 | 117 | 0.43 | 0.77 | 22 | empty |
| 4 | 60 | 0.37 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1312 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 modified (engineered).
Compared structures
- 2IHY · Structure of the Staphylococcus aureus putative ATPase subunit of an ATP-binding cassette… · 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 Q5HE50
- Elsewhere: RCSB PDB 2IHY · PDBe 2IHY · UniProt Q5HE50
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