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Crystal structure of CRISPR-associated protein

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

PDB: 4Q2C
Type: protein
Length: 926 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CRISPR-associated helicase CAS3
UniProt: D1CGD0
Ligands: NI
Pockets: 9 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CRISPR-associated helicase CAS3	protein	926	46% helix, 13% strand	D1CGD0

Ligands and binding sites

NI · Nickel (II) ion · metal · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	785	0.85	0.88	71	empty
2	259	0.78	0.91	34	empty
3	487	0.74	0.83	56	empty
4	156	0.45	0.76	29	empty
5	93	0.43	0.79	17	empty

Modifications

Observed in the structure: 19 modified (engineered).

Compared structures

4Q2C · Crystal structure of CRISPR-associated protein · 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 D1CGD0
Elsewhere: RCSB PDB 4Q2C · PDBe 4Q2C · UniProt D1CGD0

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