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Structure of anti-CRISPR ACRIIC3 and NMECAS9 hnh

Analyse Structure of anti-CRISPR ACRIIC3 and NMECAS9 hnh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6JHW
Type: protein
Length: 508 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ACRIIC3; CRISPR-associated endonuclease CAS9
EC: 3.1.-.-
UniProt: A0A0T7L299
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	ACRIIC3	protein	116	42% helix, 28% strand	—
B, D	CRISPR-associated endonuclease CAS9 (EC 3.1.-.-)	protein	138	46% helix, 9% strand	A0A0T7L299

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	855	0.68	0.74	70	empty
2	80	0.30	0.73	19	empty
3	65	0.29	0.74	17	empty

Interfaces

5 interfaces between chains.

A–B · 1066 Å² buried · 16 hydrogen bonds · protein-protein
C–D · 1048 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 502 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 123 Å² buried · 0 hydrogen bonds · protein-protein
A–C · 67 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6JHW · Structure of anti-CRISPR AcrIIC3 and NmeCas9 HNH · 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 A0A0T7L299
Elsewhere: RCSB PDB 6JHW · PDBe 6JHW · UniProt A0A0T7L299

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