Research workbench

Hnh nuclease from S. pyogenes CAS9

Analyse Hnh nuclease from S. pyogenes CAS9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6O56
Type: protein
Length: 270 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CRISPR-associated endonuclease CAS9/CSN1
EC: 3.1.-.-
UniProt: Q99ZW2
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	CRISPR-associated endonuclease CAS9/CSN1 (EC 3.1.-.-)	protein	135	53% helix, 7% strand	Q99ZW2

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	89	0.36	0.75	23	empty
2	69	0.35	0.77	21	empty

Interfaces

1 interface between chains.

A–B · 797 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

6O56 · HNH Nuclease from S. pyogenes Cas9 · the same entry in another collection · chain A against A, TM-score 1.00
Q99ZW2 · AlphaFold monomer V2.0 prediction for CRISPR-associated endonuclease CAS9/CSN1 (Q99ZW2) · a predicted model of the same protein · chain B against A, TM-score 0.96

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 Q99ZW2
Elsewhere: RCSB PDB 6O56 · PDBe 6O56 · UniProt Q99ZW2

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