Research workbench
Negative-stain electron microscopy of E. COLI clpb mutant E432A (bap form bound to clpp)
Analyse Negative-stain electron microscopy of E. COLI clpb mutant E432A (bap form bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4D2Q
- Type
- protein
- Length
- 4,734 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P63284
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 789 | — | P63284 |
Compared structures
- 4D2Q · Negative-stain electron microscopy of E. coli ClpB mutant E432A (BAP form bound to ClpP) · the same entry in another collection · chain F against F, TM-score 1.00
- P63284 · AlphaFold monomer V2.0 prediction for chaperone protein clpb (P63284) · a predicted model of the same protein · chain B against A, TM-score 0.56
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 P63284
- Elsewhere: RCSB PDB 4D2Q · PDBe 4D2Q · UniProt P63284
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