Research workbench
Structure of the zbd-xb complex
Analyse Structure of the zbd-xb complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DS8
- Type
- protein
- Length
- 96 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease ATP-binding subunit clpx; Sspb-tail peptide
- UniProt
- P0A6H1
- Ligands
- ZN
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent clp protease ATP-binding subunit clpx | protein | 43 | 28% helix, 19% strand | P0A6H1 |
| P, Q | Sspb-tail peptide | protein | 6 | 0% helix, 33% strand | — |
| B | ATP-dependent clp protease ATP-binding subunit clpx | protein | 41 | 39% helix, 24% strand | P0A6H1 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
5 interfaces between chains.
- A–B · 718 Ų buried · 3 hydrogen bonds · protein-protein
- P–B · 384 Ų buried · 10 hydrogen bonds · protein-protein
- A–Q · 356 Ų buried · 7 hydrogen bonds · protein-protein
- B–Q · 159 Ų buried · 0 hydrogen bonds · protein-protein
- A–P · 145 Ų buried · 0 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 P0A6H1
- Elsewhere: RCSB PDB 2DS8 · PDBe 2DS8 · UniProt P0A6H1
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