Research workbench
ATCLPS1-peptide complex
Analyse ATCLPS1-peptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7D34
- Type
- protein
- Length
- 160 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease adapter protein CLPS1, chloroplastic
- UniProt
- Q9SX29
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent clp protease adapter protein CLPS1, chloroplastic | protein | 81 | 47% helix, 23% strand | Q9SX29 |
| B | ATP-dependent clp protease adapter protein CLPS1, chloroplastic | protein | 79 | 48% helix, 25% strand | Q9SX29 |
Ligands and binding sites
- ACY · Acetic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 665 Ų buried · 16 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 Q9SX29
- Elsewhere: RCSB PDB 7D34 · PDBe 7D34 · UniProt Q9SX29
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