MolNFT v1 · #82085 · protein

Exploitation of hydrogen bonding constraints and flat hydrophobic energy landscapes in pim-1 kinase needle screening and inhibitor design

3VBQ · SERINE/THREONINE-protein kinase pim-1: “Exploitation of hydrogen bonding constraints and flat hydrophobic energy landscapes in pim-1 kinase needle…”. X-ray diffraction, 1 ligand (0F5), 1 pocket (best druggability 0.70). MolNFT v1…

PDB: 3VBQ
Type: protein
Length: 271 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein kinase pim-1
EC: 2.7.11.1
UniProt: P11309
Ligands: 0F5
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein kinase pim-1 (EC 2.7.11.1)	protein	271	39% helix, 24% strand	P11309

Ligands and binding sites

0F5 · (5~{Z})-5-[[3-[6-[(4-azanylcyclohexyl)amino]pyrazin-2-yl]phenyl]methylidene]-1,3-thiazolidine-2,4-dione · 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	375	0.70	0.82	50	0F5

Compared structures

3VBQ · Exploitation of hydrogen bonding constraints and flat hydrophobic energy landscapes in… · 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 P11309
Elsewhere: RCSB PDB 3VBQ · PDBe 3VBQ · UniProt P11309

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