Research workbench
Crystal structure of clpa, an HSP100 chaperone and regulator of clpap protease: structural basis of differences in function of the two aaa+ ATPase domains
Analyse Crystal structure of clpa, an HSP100 chaperone and regulator of clpap protease… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KSF
- Type
- protein
- Length
- 714 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease ATP-binding subunit clpa
- UniProt
- P0ABH9
- Ligands
- ADP, MET, MG
- Pockets
- 9 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | ATP-dependent clp protease ATP-binding subunit clpa | protein | 714 | 48% helix, 12% strand | P0ABH9 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains X
- MET · Methionine · ligand · chains X
- MG · Magnesium ion · metal · 2 copies · chains X
- IPA · Isopropyl alcohol · additive · 5 copies · chains X
- PGE · Triethylene glycol · additive · 2 copies · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 395 | 0.63 | 0.78 | 36 | empty |
| 2 | 279 | 0.61 | 0.80 | 29 | MG, ADP |
| 3 | 314 | 0.57 | 0.76 | 42 | ADP |
| 4 | 213 | 0.53 | 0.78 | 36 | empty |
| 5 | 140 | 0.44 | 0.76 | 29 | empty |
Compared structures
- 1KSF · Crystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease… · the same entry in another collection · chain X against X, TM-score 1.00
- P0ABH9 · AlphaFold monomer V2.0 prediction for ATP-dependent clp protease ATP- binding subunit… · a predicted model of the same protein · chain X against A, TM-score 0.57
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 P0ABH9
- Elsewhere: RCSB PDB 1KSF · PDBe 1KSF · UniProt P0ABH9
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