Structure of PDB 2xno Chain A

Receptor sequence
>2xnoA (length=251) Species: 9606 (Homo sapiens) [Search protein sequence]
SRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQML
VSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCEGGDLASVITKGT
KERQYLDEEFVLRVMTQLTLALKECHRRSRDLKPANVFLDGKQNVKLGDF
FVGTPYYMSPEQMNRNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKI
REGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPLILEHHHHH
H
3D structure
PDB2xno 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
Resolution1.98 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) D131 K133 A135 N136 D149 T154
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 ED8 A I14 C22 K37 M86 Y88 C89 D93 A145 F148 D159 I12 C20 K35 M84 Y86 C87 D91 A135 F138 D149 MOAD: ic50=1.18uM
PDBbind-CN: -logKd/Ki=5.93,IC50=1.18uM
BindingDB: IC50=1180nM
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:2xno, PDBe:2xno, PDBj:2xno
PDBsum2xno
PubMed21366329
UniProtP51955|NEK2_HUMAN Serine/threonine-protein kinase Nek2 (Gene Name=NEK2)

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