Research workbench
Sulfolobus solfataricus acylphosphatase. triclinic space group
Analyse Sulfolobus solfataricus acylphosphatase. triclinic space group in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BJD
- Type
- protein
- Length
- 180 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acylphosphatase
- EC
- 3.6.1.7
- UniProt
- Q97ZL0
- Ligands
- CD, CL, SO4
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acylphosphatase (EC 3.6.1.7) | protein | 90 | 24% helix, 43% strand | Q97ZL0 |
Ligands and binding sites
- CD · Cadmium ion · metal · 6 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 445 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
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 Q97ZL0
- Elsewhere: RCSB PDB 2BJD · PDBe 2BJD · UniProt Q97ZL0
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