Research workbench
X-ray structure of the DNA-eco ri endonuclease-DNA recognition complex: the recognition network and the integration of recognition and cleavage
Analyse X-ray structure of the DNA-eco ri endonuclease-DNA recognition complex: the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ERI
- Type
- protein + DNA
- Length
- 274 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00642
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | dna | 13 | — | — |
| A | — | protein | 261 | — | P00642 |
Compared structures
- 1ERI · X-ray structure of the DNA-eco ri endonuclease-DNA recognition complex: the recognition… · the same entry in another collection · chain B against B, TM-score 1.00
- P00642 · AlphaFold monomer V2.0 prediction for type-2 restriction enzyme ecori (P00642) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00642
- Elsewhere: RCSB PDB 1ERI · PDBe 1ERI · UniProt P00642
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