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Double-stranded Endonuclease Activity in B. halodurans Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR)-associated Cas2 Protein

Analyse Double-stranded Endonuclease Activity in B. halodurans Clustered Regularly… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ES1
Type: protein
Length: 95 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.1
Source: Bacillus halodurans
Molecule: BH0342 protein
EC: 3.1.-.-
UniProt: Q9KFX8
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · resolution 1.1 · 1 distinct chain · 31% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BH0342 protein (EC 3.1.-.-)	protein	95	31% helix, 27% strand	Q9KFX8

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	52	0.29	0.75	13	empty

Compared structures

4ES1 · Double-stranded endonuclease activity in B. halodurans clustered regularly interspaced… · the same entry in another collection · chain A against A, TM-score 1.00
Q9KFX8 · AlphaFold monomer V2.0 prediction for CRISPR-associated endonuclease CAS2 (Q9KFX8) · a predicted model of the same protein · chain A against A, TM-score 0.77

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 Q9KFX8
Elsewhere: RCSB PDB 4ES1 · PDBe 4ES1 · UniProt Q9KFX8

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