Research workbench
Structure of the hyperactive clpb mutant K476C, bound to casein, post- state
Analyse Structure of the hyperactive clpb mutant K476C, bound to casein, post- state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OAY
- Type
- protein
- Length
- 3,412 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Ligands
- AGS, ADP
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, E, D, B | — | protein | 570 | — | — |
| F | — | protein | 558 | — | — |
| A | — | protein | 548 | — | — |
| P | — | protein | 26 | — | — |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 7 copies · chains C, B, E, D, A
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains F, E, B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6OAY · Structure of the hyperactive ClpB mutant K476C, bound to casein, post-state · the same entry in another collection · chain F against F, 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
- Elsewhere: RCSB PDB 6OAY · PDBe 6OAY
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