Research workbench
Crystal structure of catalytically inactive FNCAS12 mutant bound to an R-loop structure containing a pre-crrna mimic and full-length DNA target
Analyse Crystal structure of catalytically inactive FNCAS12 mutant bound to an R-loop… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NFV
- Type
- protein + DNA + RNA
- Length
- 1,359 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0Q7Q2
- Ligands
- MG
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1258 | — | A0Q7Q2 |
| B | — | rna | 40 | — | — |
| C | — | dna | 37 | — | — |
| D | — | dna | 24 | — | — |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A, B
- B3P · 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-propane-1,3-diol · additive · chains A, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NFV · Crystal structure of catalytically inactive FnCas12 mutant bound to an R-loop structure… · the same entry in another collection · chain A against A, TM-score 1.00
- A0Q7Q2 · AlphaFold monomer V2.0 prediction for CRISPR-associated endonuclease CAS12A (A0Q7Q2) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 A0Q7Q2
- Elsewhere: RCSB PDB 5NFV · PDBe 5NFV · UniProt A0Q7Q2
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