Research workbench
Crystal structure of the C-terminal fragment of AAA+ATPASE from haemophilus influenzae
Analyse Crystal structure of the C-terminal fragment of AAA+ATPASE from haemophilus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BGE
- Type
- protein
- Length
- 326 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Predicted ATPase
- UniProt
- Q4QL22
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Predicted ATPase | protein | 163 | 67% helix, 0% strand | Q4QL22 |
| B | Predicted ATPase | protein | 163 | 66% helix, 0% strand | Q4QL22 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 517 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 3BGE · Crystal structure of the C-terminal fragment of AAA+ATPase from Haemophilus influenzae · 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 Q4QL22
- Elsewhere: RCSB PDB 3BGE · PDBe 3BGE · UniProt Q4QL22
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