MolNFT v1 · #127711 · protein

Crystal structure of human pim-1 kinase in complex with a consensuspeptide and fragment like molekule (E)-3-(P-TOLYL)ACRYLIC acid

5N4O · SERINE/THREONINE-protein kinase pim-1: “Crystal structure of human pim-1 kinase in complex with a consensuspeptide and fragment like molekule…”. X-ray diffraction, 1 ligand (8MB), 1 pocket (best druggability 0.68). MolNFT v1 #127711…

PDB: 5N4O
Type: protein
Length: 280 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein kinase pim-1; Pimtide
EC: 2.7.11.1
UniProt: P11309
Ligands: 8MB
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein kinase pim-1 (EC 2.7.11.1)	protein	271	41% helix, 23% strand	P11309
B	Pimtide	protein	9	0% helix, 0% strand	—

Ligands and binding sites

8MB · (~{E})-3-(4-methylphenyl)prop-2-enoic acid · 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	472	0.68	0.79	49	8MB

Interfaces

1 interface between chains.

A–B · 586 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

5N4O · Crystal structure of human Pim-1 kinase in complex with a consensuspeptide and fragment… · 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 5N4O · PDBe 5N4O · UniProt P11309

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