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Crystal structure of amppnp bound CK1A alpha from C. neoformans

Analyse Crystal structure of amppnp bound CK1A alpha from C. neoformans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6K74
Type: protein
Length: 330 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Casein kinase II subunit alpha
UniProt: A0A226BA59
Ligands: ANP, MG, SO4
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Casein kinase II subunit alpha	protein	330	44% helix, 15% strand	A0A226BA59

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
MG · Magnesium ion · metal · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

2 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	502	0.72	0.81	54	ANP, MG, SO4
2	55	0.40	0.81	14	empty

Compared structures

6K74 · Crystal structure of AMPPNP bound Ck1a alpha from C. neoformans · 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 A0A226BA59
Elsewhere: RCSB PDB 6K74 · PDBe 6K74 · UniProt A0A226BA59

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