Structure of PDB 2xnm Chain A

Receptor sequence
>2xnmA (length=258) Species: 9606 (Homo sapiens) [Search protein sequence]
SRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQML
VSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCEGGDLASVITKGT
KERQYLDEEFVLRVMTQLTLALKECHRRRDLKPANVFLDGKQNVKLGDFG
LARILFVGTPYYMSPEQMNRSYNEKSDIWSLGCLLYELCALMPPFTAFSQ
KELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPLI
LEHHHHHH
3D structure
PDB2xnm 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
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D141 K143 A145 N146 D159 T179
Catalytic site (residue number reindexed from 1) D130 K132 A134 N135 D148 T159
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 WGZ A I14 C22 K37 Y88 C89 D93 F148 G158 D159 I12 C20 K35 Y86 C87 D91 F137 G147 D148 MOAD: ic50=0.16uM
PDBbind-CN: -logKd/Ki=6.80,IC50=0.16uM
BindingDB: IC50=25nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2xnm, PDBe:2xnm, PDBj:2xnm
PDBsum2xnm
PubMed21366329
UniProtP51955|NEK2_HUMAN Serine/threonine-protein kinase Nek2 (Gene Name=NEK2)

[Back to BioLiP]