Structure of PDB 2j51 Chain A

Receptor sequence
>2j51A (length=288) Species: 9606 (Homo sapiens) [Search protein sequence]
YEHVTRDLNPEDFWEIIGELGDGAFGKVYKAQNKETSVLAAAKVIDTKSE
EELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVM
LELERPLTESQIQVVCKQTLDALNYLHDNKIIHRDLKAGNILFTLDGDIK
LADFGVSAKNTRTIQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWS
LGITLIEMAEIEPPHHELNPMRVLLKIAKSEPPTLAQPSRWSSNFKDFLK
KCLEKNVDARWTTSQLLQHPFVTVDSNKPIRELIAEAK
3D structure
PDB2j51 Activation Segment Dimerization: A Mechanism for Kinase Autophosphorylation of Non-Consensus Sites.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D155 K157 G159 N160 D173 R182 T193
Catalytic site (residue number reindexed from 1) D135 K137 G139 N140 D153 R162 T173
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 DKI A L40 V48 A61 I108 F110 C111 G114 L162 D173 L20 V28 A41 I88 F90 C91 G94 L142 D153
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:2j51, PDBe:2j51, PDBj:2j51
PDBsum2j51
PubMed18239682
UniProtQ9H2G2|SLK_HUMAN STE20-like serine/threonine-protein kinase (Gene Name=SLK)

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