MolNFT v1 · #13890 · protein

Room temperature crystal structure of the apo-form of the catalytic subunit of protein kinase CK2 from zea mays

1LR4: “Room temperature crystal structure of the apo-form of the catalytic subunit of protein kinase CK2 from zea…”. X-ray diffraction, 1 ligand (BEN), 1 pocket (best druggability 0.64). MolNFT v1 #13890 on GenesisL1: 3D structure, binding…

PDB: 1LR4
Type: protein
Length: 327 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein kinase CK2
EC: 2.7.1.37
UniProt: P28523
Ligands: BEN
Pockets: 1 · best druggability 0.64

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein kinase CK2 (EC 2.7.1.37)	protein	327	44% helix, 15% strand	P28523

Ligands and binding sites

BEN · Benzamidine · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	319	0.64	0.80	42	BEN

Compared structures

1LR4 · Room Temperature Crystal Structure of the Apo-form of the catalytic subunit of protein… · the same entry in another collection · chain A against A, TM-score 1.00
P28523 · AlphaFold monomer V2.0 prediction for casein kinase II subunit alpha (P28523) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P28523
Elsewhere: RCSB PDB 1LR4 · PDBe 1LR4 · UniProt P28523

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