MolNFT v1 · #23374 · protein
The structure of clpp at 2.3 ångström resolution suggests a model for ATP-dependent proteolysis
1TYF: “The structure of clpp at 2.3 ångström resolution suggests a model for ATP-dependent proteolysis”. X-ray diffraction. MolNFT v1 #23374 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1TYF
- Type
- protein
- Length
- 2,562 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0A6G7
Structure
x-ray diffraction · 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 | 183 | — | P0A6G7 |
Compared structures
- 1TYF · The structure of clpp at 2.3 ångström resolution suggests a model for ATP-dependent… · the same entry in another collection · chain K against K, 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 P0A6G7
- Elsewhere: RCSB PDB 1TYF · PDBe 1TYF · UniProt P0A6G7
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