Structure of PDB 4a4x Chain A

Receptor sequence
>4a4xA (length=253) Species: 9606 (Homo sapiens) [Search protein sequence]
SRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQML
VSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCEGGDLASVITKGT
KERQYLDEEFVLRVMTQLTLALKECHRRSHRDLKPANVFLDGKQNVKLGD
FGLVGTPYYMSPEQMNRNEKSDIWSLGCLLYELCALMPPFTAFSQKELAG
KIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPLILEHHH
HHH
3D structure
PDB4a4x Design of Potent and Selective Hybrid Inhibitors of the Mitotic Kinase Nek2: Structure-Activity Relationship, Structural Biology, and Cellular Activity.
ChainA
Resolution2.4 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) D132 K134 A136 N137 D150 T156
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 JUP A I14 G15 Y19 C22 V35 M86 Y88 C89 F148 G158 D159 F160 I12 G13 Y17 C20 V33 M84 Y86 C87 F139 G149 D150 F151 MOAD: ic50=0.059uM
PDBbind-CN: -logKd/Ki=7.23,IC50=0.059uM
BindingDB: IC50=2700nM
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:4a4x, PDBe:4a4x, PDBj:4a4x
PDBsum4a4x
PubMed22404346
UniProtP51955|NEK2_HUMAN Serine/threonine-protein kinase Nek2 (Gene Name=NEK2)

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