Research workbench
Cryo-EM structure of type I-F CRISPR crrna-guided csy surveillance complex with bound target dsdna
Analyse Cryo-EM structure of type I-F CRISPR crrna-guided csy surveillance complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B44
- Type
- protein + DNA + RNA
- Length
- 2,993 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR-associated protein CSY1; CRISPR-associated protein CSY2; CRISPR-associated protein…
- EC
- 3.1.-.-
- UniProt
- Q02ML9, Q02MM0, Q02MM1, Q02MM2
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 10 distinct chains · 24% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRISPR-associated protein CSY1 | protein | 424 | 36% helix, 8% strand | Q02ML9 |
| B | CRISPR-associated protein CSY2 | protein | 305 | 17% helix, 27% strand | Q02MM0 |
| C | CRISPR-associated protein CSY3 | protein | 293 | 23% helix, 12% strand | Q02MM1 |
| D, G, H | CRISPR-associated protein CSY3 | protein | 333 | 20% helix, 20% strand | Q02MM1 |
| E | CRISPR-associated protein CSY3 | protein | 334 | 25% helix, 24% strand | Q02MM1 |
| F | CRISPR-associated protein CSY3 | protein | 335 | 24% helix, 26% strand | Q02MM1 |
| L | CRISPR-associated endonuclease CAS6/CSY4 (EC 3.1.-.-) | protein | 189 | 17% helix, 6% strand | Q02MM2 |
| M | Pseudomonas aeruginosa strain SMC4485 CRISPR repeat sequence | rna | 60 | — | — |
| N | Target DNA strand (41-mer) | dna | 41 | — | — |
| O | Non-target DNA strand (5'- D(P*CP*AP*GP*TP*CP*AP*TP*CP*AP*CP*CP*AP*A)-3') | dna | 13 | — | — |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1077 | 0.86 | 0.87 | 122 | empty |
| 2 | 1060 | 0.84 | 0.85 | 142 | empty |
| 3 | 593 | 0.80 | 0.86 | 78 | empty |
| 4 | 926 | 0.80 | 0.82 | 104 | empty |
| 5 | 761 | 0.78 | 0.82 | 78 | empty |
Interfaces
33 interfaces between chains.
- A–B · 3400 Ų buried · 28 hydrogen bonds · protein-protein
- G–H · 1946 Ų buried · 20 hydrogen bonds · protein-protein
- F–G · 1941 Ų buried · 20 hydrogen bonds · protein-protein
- D–E · 1925 Ų buried · 20 hydrogen bonds · protein-protein
- E–F · 1854 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 6B44 · Cryo-EM structure of Type I-F CRISPR crRNA-guided Csy surveillance complex with bound… · the same entry in another collection · chain O against O, 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 Q02ML9
- Every structure of UniProt Q02MM0
- Every structure of UniProt Q02MM1
- Every structure of UniProt Q02MM2
- Elsewhere: RCSB PDB 6B44 · PDBe 6B44 · UniProt Q02ML9 · UniProt Q02MM0 · UniProt Q02MM1 · UniProt Q02MM2
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