MolNFT v1 · #113154 · protein
Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product
5A6S: “Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation…”. X-ray diffraction. MolNFT v1 #113154 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5A6S
- Type
- protein
- Length
- 352 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D9ZNF3
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 273 | — | D9ZNF3 |
| B | — | protein | 79 | — | D9ZNF3 |
Compared structures
- 5A6S · Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a… · 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 D9ZNF3
- Elsewhere: RCSB PDB 5A6S · PDBe 5A6S · UniProt D9ZNF3
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