Structure of PDB 4lgd Chain C

Receptor sequence
>4lgdC (length=349) Species: 9606 (Homo sapiens) [Search protein sequence]
KKLSEDSLTKQPEEVFDVLEKSVFKAIHKESGQVVAIKQVPVESDLQEII
KEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTL
IEDEIATILKSTLKGLEYLHFMRKIHRNIKAGNILLNTEGHAKLADFGVA
GQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITSIEMAEGK
PPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKNPEQRAT
ATQLLQHPFIKNAKPVSILRDLITEAMEIKAKRHEEQQRELEEEEFDFLK
NLSLEELQMRLKALDPMMEREIEELRQRYTAKRQPILDAMDAKKRRQQN
3D structure
PDB4lgd Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5.
ChainC
Resolution3.05 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) N146 K148 G150 N151 D164 D173 T184
Catalytic site (residue number reindexed from 1) N128 K130 G132 N133 D146 D155 T166
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 ANP C V41 A54 C102 D109 D164 V23 A36 C84 D91 D146
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
GO:0007165 signal transduction

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4lgd, PDBe:4lgd, PDBj:4lgd
PDBsum4lgd
PubMed23972470
UniProtQ13188|STK3_HUMAN Serine/threonine-protein kinase 3 (Gene Name=STK3)

[Back to BioLiP]