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Crystal structure of CAS2

Analyse Crystal structure of CAS2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6JHZ
Type: protein
Length: 189 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CRISPR-associated endoribonuclease CAS2; 5-mer peptide
EC: 3.1.-.-
UniProt: Q73QW4
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 3 distinct chains · 36% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CRISPR-associated endoribonuclease CAS2 (EC 3.1.-.-)	protein	93	37% helix, 29% strand	Q73QW4
B	CRISPR-associated endoribonuclease CAS2 (EC 3.1.-.-)	protein	91	37% helix, 26% strand	Q73QW4
Q	5-mer peptide	protein	5	0% helix, 0% strand	—

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	111	0.44	0.78	19	empty

Interfaces

1 interface between chains.

A–B · 1645 Å² buried · 40 hydrogen bonds · protein-protein

Compared structures

6JHZ · Crystal structure of cas2 · the same entry in another collection · chain A against A, TM-score 1.00
Q73QW4 · AlphaFold monomer V2.0 prediction for CRISPR-associated endoribonuclease CAS2 (Q73QW4) · a predicted model of the same protein · chain B against A, TM-score 0.89

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 Q73QW4
Elsewhere: RCSB PDB 6JHZ · PDBe 6JHZ · UniProt Q73QW4

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