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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: 4F3M
Type: protein
Length: 429 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BH0337 protein
UniProt: Q9KFY3
Ligands: SO4
Pockets: 7 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 19% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BH0337 protein	protein	213	19% helix, 42% strand	Q9KFY3
B	BH0337 protein	protein	216	19% helix, 42% strand	Q9KFY3

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A, B
EDO · 1,2-ethanediol · additive · 6 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	74	0.69	0.94	22	empty
2	302	0.67	0.82	32	SO4
3	243	0.65	0.83	51	empty
4	280	0.55	0.76	44	empty
5	184	0.44	0.74	24	empty

Interfaces

1 interface between chains.

A–B · 2342 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4F3M · 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 Q9KFY3
Elsewhere: RCSB PDB 4F3M · PDBe 4F3M · UniProt Q9KFY3

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