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Cryo EM structure of anti-crisprs, ACRF1 and ACRF2, bound to type I-F crrna-guided CRISPR surveillance complex

Analyse Cryo EM structure of anti-crisprs, ACRF1 and ACRF2, bound to type I-F… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UZ9
Type: protein + RNA
Length: 3,179 residues
Chains: 13
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CRISPR-associated protein CSY1; CRISPR-associated protein CSY2; CRISPR-associated protein…
EC: 3.1.-.-
UniProt: Q02ML9, Q02MM0, Q02MM1, L7P7M1, Q6TM72, Q02MM2
Pockets: 20 · best druggability 0.85

Structure

electron microscopy · 10 distinct chains · 27% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CRISPR-associated protein CSY1	protein	424	43% helix, 6% strand	Q02ML9
B	CRISPR-associated protein CSY2	protein	305	20% helix, 24% strand	Q02MM0
C	CRISPR-associated protein CSY3	protein	293	25% helix, 23% strand	Q02MM1
D, G, H	CRISPR-associated protein CSY3	protein	333	24% helix, 23% strand	Q02MM1
E	CRISPR-associated protein CSY3	protein	334	24% helix, 22% strand	Q02MM1
F	CRISPR-associated protein CSY3	protein	335	24% helix, 23% strand	Q02MM1
I, J	Anti-CRISPR protein ACR30-35	protein	76	25% helix, 37% strand	L7P7M1
K	Anti-CRISPR protein 30	protein	88	27% helix, 23% strand	Q6TM72
L	CRISPR-associated endonuclease CAS6/CSY4 (EC 3.1.-.-)	protein	189	23% helix, 13% strand	Q02MM2
M	CRISPR RNA (60-mer)	rna	60	—	—

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1056	0.85	0.86	133	empty
2	798	0.84	0.87	81	empty
3	1062	0.83	0.84	100	empty
4	1141	0.83	0.84	122	empty
5	1054	0.83	0.84	115	empty

Interfaces

34 interfaces between chains.

A–B · 4438 Å² buried · 53 hydrogen bonds · protein-protein
F–G · 2060 Å² buried · 22 hydrogen bonds · protein-protein
C–D · 1989 Å² buried · 23 hydrogen bonds · protein-protein
D–E · 1935 Å² buried · 19 hydrogen bonds · protein-protein
E–F · 1893 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

5UZ9 · Cryo EM structure of anti-CRISPRs, AcrF1 and AcrF2, bound to type I-F crRNA-guided CRISPR… · the same entry in another collection · chain M against M, 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 Q02ML9
Every structure of UniProt Q02MM0
Every structure of UniProt Q02MM1
Every structure of UniProt L7P7M1
Every structure of UniProt Q6TM72
Every structure of UniProt Q02MM2
Elsewhere: RCSB PDB 5UZ9 · PDBe 5UZ9 · UniProt Q02ML9 · UniProt Q02MM0 · UniProt Q02MM1 · UniProt L7P7M1 · UniProt Q6TM72 · UniProt Q02MM2

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