Research workbench
Crystal structure of the I-crei homing endonuclease D75N variant in complex with its target DNA in the presence of manganese
Analyse Crystal structure of the I-crei homing endonuclease D75N variant in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FB7
- Type
- protein + DNA
- Length
- 352 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P05725
- Ligands
- MN
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 152 | — | P05725 |
| D, F | — | dna | 14 | — | — |
| E, G | — | dna | 10 | — | — |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 3 copies · chains A, B, D, E, F, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6FB7 · Crystal Structure of the I-CreI Homing Endonuclease D75N variant in complex with its… · the same entry in another collection · chain G against G, TM-score 1.00
- P05725 · AlphaFold monomer V2.0 prediction for DNA endonuclease I-crei (P05725) · a predicted model of the same protein · chain B 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 P05725
- Elsewhere: RCSB PDB 6FB7 · PDBe 6FB7 · UniProt P05725
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