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Crystal structure of the human PIM1 in complex with amppnp and pimtide

Analyse Crystal structure of the human PIM1 in complex with amppnp and pimtide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BZK
Type: protein
Length: 275 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pimtide; Proto-oncogene serine threonine protein kinase PIM1
EC: 2.7.1.37
UniProt: P11309
Ligands: ANP
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pimtide	protein	7	0% helix, 0% strand	—
B	Proto-oncogene serine threonine protein kinase PIM1 (EC 2.7.1.37)	protein	268	40% helix, 22% strand	P11309

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains B

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	271	0.60	0.79	32	ANP
2	115	0.41	0.77	19	empty

Interfaces

1 interface between chains.

A–B · 514 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

2BZK · Crystal structure of the human PIM1 in complex with amppnp and pimtide · 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 2BZK · PDBe 2BZK · UniProt P11309

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