MolNFT v1 · #8830 · protein

Human cyclin-dependent kinase 2

1HCK: “Human cyclin-dependent kinase 2”. X-ray diffraction, 2 ligands (ATP, MG), 3 pockets (best druggability 0.69). MolNFT v1 #8830 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1HCK
Type: protein
Length: 294 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Human cyclin-dependent kinase 2
EC: 2.7.1.37
UniProt: P24941
Ligands: ATP, MG
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Human cyclin-dependent kinase 2 (EC 2.7.1.37)	protein	294	34% helix, 16% strand	P24941

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

3 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	303	0.69	0.83	37	MG, ATP
2	83	0.34	0.74	17	empty
3	61	0.29	0.74	16	empty

Compared structures

1HCK · Human cyclin-dependent kinase 2 · the same entry in another collection · chain A against A, TM-score 1.00
P24941 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinase 2 (P24941) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P24941
Elsewhere: RCSB PDB 1HCK · PDBe 1HCK · UniProt P24941

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