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Crystal structure of NMECAS9 hnh domain bound to anti-CRISPR ACRIIC1

Analyse Crystal structure of NMECAS9 hnh domain bound to anti-CRISPR ACRIIC1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VGB
Type: protein
Length: 225 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CRISPR-associated endonuclease CAS9; Anti-CRISPR protein (ACRIIC1)
EC: 3.1.-.-
UniProt: X5EPV9
Ligands: SO4
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CRISPR-associated endonuclease CAS9 (EC 3.1.-.-)	protein	140	55% helix, 9% strand	X5EPV9
B	Anti-CRISPR protein (ACRIIC1)	protein	85	26% helix, 36% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 3 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	331	0.63	0.79	51	GOL

Interfaces

1 interface between chains.

A–B · 1038 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

5VGB · Crystal structure of NmeCas9 HNH domain bound to anti-CRISPR AcrIIC1 · the same entry in another collection · chain A against A, 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 X5EPV9
Elsewhere: RCSB PDB 5VGB · PDBe 5VGB · UniProt X5EPV9

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