Structure of PDB 3tku Chain A

Receptor sequence
>3tkuA (length=395) Species: 9606 (Homo sapiens) [Search protein sequence]
SAKVRLKKLEQLLLDGPWRNESALSVETLLDVLVCLYTECSHSALRRDKY
VAEFLEWAKPFTQLVKEMQLHREDFEIIKVIGRGAFGEVAVVKMKNTERI
YAMKILNKWEMLKRAETACFREERDVLVNGDCQWITALHYAFQDENHLYL
VMDYYVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIDSIHQLHYVHRDI
KPDNVLLDVNGHIRLADFGSCLKMNDDGTVQSSVAVGTPDYISPEILQAM
EDGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQ
FPSHVTDVSEEAKDLIQRLICSRERRLGQNGIEDFKKHAFFEGLNWENIR
NLEAPYIPDVSSPSDTSNFDVSGLHLPFIGFTFTTESCFSDRGSL
3D structure
PDB3tku Co-crystal structures of inhibitors with MRCK, a key regulator of tumor cell invasion
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D200 K202 N205 D218 T239
Catalytic site (residue number reindexed from 1) D199 K201 N204 D217 T238
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 M77 A I82 G83 V90 A103 Y155 D204 N205 L207 F370 I81 G82 V89 A102 Y154 D203 N204 L206 F369 MOAD: ic50=1.92uM
PDBbind-CN: -logKd/Ki=5.72,IC50=1.92uM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine 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:3tku, PDBe:3tku, PDBj:3tku
PDBsum3tku
PubMed21949762
UniProtQ9Y5S2|MRCKB_HUMAN Serine/threonine-protein kinase MRCK beta (Gene Name=CDC42BPB)

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