Structure of PDB 2xnn Chain A

Receptor sequence
>2xnnA (length=251) Species: 9606 (Homo sapiens) [Search protein sequence]
SRAEDYEVLYTIGTYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQMLVS
EVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCEGGDLASVITKGTKE
RQYLDEEFVLRVMTQLTLALKECHRRSRDLKPANVFLDGKQNVKLGDFGF
VGTPYYMSPEQMNRYNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKI
REGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPLILEHHHHH
H
3D structure
PDB2xnn Benzimidazole Inhibitors Induce a Dfg-Out Conformation of Never in Mitosis Gene A-Related Kinase 2 (Nek2) without Binding to the Back Pocket and Reveal a Nonlinear Structure-Activity Relationship.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D141 K143 A145 N146 D159 T179
Catalytic site (residue number reindexed from 1) D129 K131 A133 N134 D147 T153
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 430 A I14 C22 K37 Y88 C89 D93 A145 F148 D159 I12 C18 K33 Y84 C85 D89 A133 F136 D147 PDBbind-CN: -logKd/Ki=4.30,IC50>50uM
BindingDB: IC50=>50000nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:2xnn, PDBe:2xnn, PDBj:2xnn
PDBsum2xnn
PubMed21366329
UniProtP51955|NEK2_HUMAN Serine/threonine-protein kinase Nek2 (Gene Name=NEK2)

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