Research workbench
DNA binding and cleavage by the giy-yig endonuclease R.ECO29KI inactive variant E142Q
Analyse DNA binding and cleavage by the giy-yig endonuclease R.ECO29KI inactive variant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MX4
- Type
- protein + DNA
- Length
- 1,856 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q46944
Structure
x-ray diffraction · 9 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 213 | — | Q46944 |
| C | — | protein | 208 | — | Q46944 |
| D | — | protein | 208 | — | Q46944 |
| E | — | protein | 211 | — | Q46944 |
| F | — | protein | 210 | — | Q46944 |
| G | — | protein | 208 | — | Q46944 |
| H | — | protein | 209 | — | Q46944 |
| I, K, M, O | — | dna | 22 | — | — |
| J, L, N, P | — | dna | 22 | — | — |
Compared structures
- 3MX4 · DNA binding and cleavage by the GIY-YIG endonuclease R.Eco29KI inactive variant E142Q · the same entry in another collection · chain N against N, 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 Q46944
- Elsewhere: RCSB PDB 3MX4 · PDBe 3MX4 · UniProt Q46944
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