Research workbench
C-terminal domain of CTP1L endolysin mutant V195P that reduces autoproteolysis
Analyse C-terminal domain of CTP1L endolysin mutant V195P that reduces autoproteolysis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CU2
- Type
- protein
- Length
- 80 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endolysin
- UniProt
- D9ZNF3
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endolysin | protein | 80 | 36% helix, 20% strand | D9ZNF3 |
Compared structures
- 4CU2 · C-terminal domain of CTP1L endolysin mutant V195P that reduces autoproteolysis · 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 4CU2 · PDBe 4CU2 · UniProt D9ZNF3
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