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Crystal structure of anti-CRISPR protein ACRF3

Analyse Crystal structure of anti-CRISPR protein ACRF3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GNF
Type: protein
Length: 272 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein ACRF3
UniProt: L7P7R7
Ligands: CA
Pockets: 4 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 68% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein ACRF3	protein	137	66% helix, 0% strand	L7P7R7
B	Uncharacterized protein ACRF3	protein	135	70% helix, 1% strand	L7P7R7

Ligands and binding sites

CA · Calcium ion · metal · 3 copies · chains A, B

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

Pockets

4 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	187	0.58	0.81	28	CA
2	69	0.33	0.76	16	empty
3	65	0.31	0.75	17	empty
4	50	0.26	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 849 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

5GNF · Crystal structure of anti-CRISPR protein AcrF3 · 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 L7P7R7
Elsewhere: RCSB PDB 5GNF · PDBe 5GNF · UniProt L7P7R7

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