Structure of PDB 4tpt Chain A

Receptor sequence
>4tptA (length=279) Species: 9606 (Homo sapiens) [Search protein sequence]
DLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKV
MRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMDPFPWQQKV
RFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVKK
RYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPR
TLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFE
ALSLYLGELGIPLPAELEELDHTVSMQYG
3D structure
PDB4tpt Discovery of a Type III Inhibitor of LIM Kinase 2 That Binds in a DFG-Out Conformation.
ChainA
Resolution2.6 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) D451 N453 H455 N456 D469 N509
Catalytic site (residue number reindexed from 1) D122 N124 H126 N127 D140 N157
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 35H A K360 I363 M380 V388 L403 L442 H449 A468 D469 F470 L472 R474 K31 I34 M51 V59 L74 L113 H120 A139 D140 F141 L143 R145 PDBbind-CN: -logKd/Ki=7.04,IC50=92nM
BindingDB: IC50=92nM
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:4tpt, PDBe:4tpt, PDBj:4tpt
PDBsum4tpt
PubMed25589930
UniProtP53671|LIMK2_HUMAN LIM domain kinase 2 (Gene Name=LIMK2)

[Back to BioLiP]