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Structure of csy-ACRIF24

Analyse Structure of csy-ACRIF24 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ELM
Type: protein + RNA
Length: 6,321 residues
Chains: 22
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Type I-F CRISPR-associated protein CSY1; CRISPR type I-F/YPEST-associated protein CSY2…
UniProt: A0A3A8DDU9, B3G161, A0A659BSG0
Pockets: 20 · best druggability 0.85

Structure

electron microscopy · 15 distinct chains · 29% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Type I-F CRISPR-associated protein CSY1	protein	417	44% helix, 7% strand	A0A3A8DDU9
B, L	CRISPR type I-F/YPEST-associated protein CSY2	protein	305	22% helix, 31% strand	B3G161
C	CRISPR-associated protein CSY3	protein	292	26% helix, 26% strand	A0A659BSG0
D, O	CRISPR-associated protein CSY3	protein	334	25% helix, 24% strand	A0A659BSG0
E	CRISPR-associated protein CSY3	protein	337	24% helix, 25% strand	A0A659BSG0
F, P	CRISPR-associated protein CSY3	protein	335	25% helix, 25% strand	A0A659BSG0
G	CRISPR-associated protein CSY3	protein	329	26% helix, 26% strand	A0A659BSG0
H	CRISPR-associated protein CSY3	protein	332	25% helix, 25% strand	A0A659BSG0
K	Type I-F CRISPR-associated protein CSY1	protein	424	44% helix, 5% strand	A0A3A8DDU9
I, S	Type I-F CRISPR-associated endoribonuclease CAS6/CSY4	protein	187	26% helix, 26% strand	—
M	CRISPR-associated protein CSY3	protein	293	26% helix, 26% strand	A0A659BSG0
N	CRISPR-associated protein CSY3	protein	335	25% helix, 24% strand	A0A659BSG0
Q, R	CRISPR-associated protein CSY3	protein	333	26% helix, 27% strand	A0A659BSG0
U, V	ACRIF24	protein	227	29% helix, 24% strand	—
J, T	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	1130	0.85	0.86	118	empty
2	1174	0.85	0.86	130	empty
3	1048	0.84	0.85	117	empty
4	784	0.82	0.85	84	empty
5	928	0.82	0.84	103	empty

Interfaces

62 interfaces between chains.

K–L · 3509 Å² buried · 33 hydrogen bonds · protein-protein
A–B · 3153 Å² buried · 30 hydrogen bonds · protein-protein
E–F · 2240 Å² buried · 32 hydrogen bonds · protein-protein
N–O · 2163 Å² buried · 33 hydrogen bonds · protein-protein
F–G · 2077 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

7ELM · Structure of Csy-AcrIF24 · 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 A0A3A8DDU9
Every structure of UniProt B3G161
Every structure of UniProt A0A659BSG0
Elsewhere: RCSB PDB 7ELM · PDBe 7ELM · UniProt A0A3A8DDU9 · UniProt B3G161 · UniProt A0A659BSG0

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