Research workbench
Structure of LBCAS12A-crrna complex bound to ACRVA4 (form B complex)
Analyse Structure of LBCAS12A-crrna complex bound to ACRVA4 (form B complex) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KLB
- Type
- protein + RNA
- Length
- 2,517 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0U2APF4
- Ligands
- MG
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1118 | — | — |
| B, C | — | protein | 117 | — | A0A0U2APF4 |
| D | — | protein | 1115 | — | — |
| E, G | — | rna | 25 | — | — |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, G, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6KLB · Structure of LbCas12a-crRNA complex bound to AcrVA4 (form B complex) · 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 A0A0U2APF4
- Elsewhere: RCSB PDB 6KLB · PDBe 6KLB · UniProt A0A0U2APF4
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