Research workbench
Protelomerase tela R205A covalently complexed with substrate DNA
Analyse Protelomerase tela R205A covalently complexed with substrate DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E0Z
- Type
- protein + DNA
- Length
- 349 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q7CWV1
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 319 | — | Q7CWV1 |
| C | — | dna | 13 | — | — |
| D | — | dna | 17 | — | — |
Compared structures
- 4E0Z · Protelomerase tela R205A covalently complexed with substrate DNA · 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 Q7CWV1
- Elsewhere: RCSB PDB 4E0Z · PDBe 4E0Z · UniProt Q7CWV1
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