Research workbench
Structure of large terminase from the thermophilic bacteriophage D6E in complex with ADP (crystal form 3)
Analyse Structure of large terminase from the thermophilic bacteriophage D6E in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OEB
- Type
- protein
- Length
- 2,424 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- E5DV50
- Ligands
- ADP, MG
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, E | — | protein | 405 | — | E5DV50 |
| C | — | protein | 402 | — | E5DV50 |
| F | — | protein | 402 | — | E5DV50 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OEB · Structure of large terminase from the thermophilic bacteriophage D6E in complex with ADP… · 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 E5DV50
- Elsewhere: RCSB PDB 5OEB · PDBe 5OEB · UniProt E5DV50
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