Research workbench
Structure of full length CMR2 from pyrococcus furiosus (manganese bound form)
Analyse Structure of full length CMR2 from pyrococcus furiosus (manganese bound form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4W8Y
- Type
- protein
- Length
- 1,663 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR system cmr subunit CMR2
- UniProt
- Q8U1S6
- Ligands
- MN, ZN
- Pockets
- 20 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRISPR system cmr subunit CMR2 | protein | 835 | 57% helix, 13% strand | Q8U1S6 |
| B | CRISPR system cmr subunit CMR2 | protein | 828 | 57% helix, 13% strand | Q8U1S6 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 8 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 514 | 0.71 | 0.80 | 54 | MN |
| 2 | 327 | 0.70 | 0.83 | 49 | MN |
| 3 | 315 | 0.70 | 0.83 | 47 | MN |
| 4 | 487 | 0.69 | 0.80 | 46 | MN |
| 5 | 197 | 0.64 | 0.84 | 36 | empty |
Interfaces
1 interface between chains.
- A–B · 210 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4W8Y · Structure of full length Cmr2 from Pyrococcus furiosus (Manganese bound form) · the same entry in another collection · chain A against A, TM-score 1.00
- Q8U1S6 · AlphaFold monomer V2.0 prediction for CRISPR system cmr subunit CMR2 (Q8U1S6) · a predicted model of the same protein · chain A 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 Q8U1S6
- Elsewhere: RCSB PDB 4W8Y · PDBe 4W8Y · UniProt Q8U1S6
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