MolNFT v1 · #11743 · protein

Crystal structure of human CDK2 (unphosphorylated) in complex with PKF049-365

1JVP · Cell division protein kinase 2: “Crystal structure of human CDK2 (unphosphorylated) in complex with PKF049-365”. X-ray diffraction, 1 ligand (89E), 2 pockets (best druggability 0.71). MolNFT v1 #11743 on GenesisL1: 3D structure…

PDB: 1JVP
Type: protein
Length: 281 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein kinase 2
EC: 2.7.1.37
UniProt: P24941
Ligands: 89E
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
P	Cell division protein kinase 2 (EC 2.7.1.37)	protein	281	36% helix, 17% strand	P24941

Ligands and binding sites

89E · 3-pyridin-4-yl-2,4-dihydroindeno[1,2-c]pyrazole · ligand · chains P

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	425	0.71	0.81	55	89E
2	59	0.34	0.77	13	empty

Compared structures

1JVP · Crystal structure of human CDK2 (unphosphorylated) in complex with PKF049-365 · the same entry in another collection · chain P against P, TM-score 1.00
P24941 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinase 2 (P24941) · a predicted model of the same protein · chain P against A, TM-score 0.96

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 1JVP · PDBe 1JVP · UniProt P24941

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