Research workbench
Clpp from neisseria meningitidis - compressed conformation
Analyse Clpp from neisseria meningitidis - compressed conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KR2
- Type
- protein
- Length
- 2,492 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A425BAU1
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N | — | protein | 178 | — | A0A425BAU1 |
Compared structures
- 7KR2 · ClpP from Neisseria meningitidis - Compressed conformation · the same entry in another collection · chain A against A, 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
- Every structure of UniProt A0A425BAU1
- Elsewhere: RCSB PDB 7KR2 · PDBe 7KR2 · UniProt A0A425BAU1
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