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The structure of NT.BSPD6I nicking endonuclease with all cysteines mutated by serine residues at 0.19 nm resolution .

Analyse The structure of NT.BSPD6I nicking endonuclease with all cysteines mutated by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LIZ
Type: protein
Length: 584 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nicking endonuclease N.BSPD6I
UniProt: Q8GCA3
Ligands: PO4
Pockets: 8 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nicking endonuclease N.BSPD6I	protein	584	60% helix, 9% strand	Q8GCA3

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A

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

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	761	0.76	0.80	82	empty
2	274	0.52	0.75	29	empty
3	180	0.46	0.75	25	empty
4	57	0.41	0.81	16	empty
5	75	0.39	0.79	21	empty

Compared structures

5LIZ · The structure of Nt.BspD6I nicking endonuclease with all cysteines mutated by serine… · 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 Q8GCA3
Elsewhere: RCSB PDB 5LIZ · PDBe 5LIZ · UniProt Q8GCA3

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