Structure of PDB 4l6q Chain B

Receptor sequence
>4l6qB (length=388) Species: 9606 (Homo sapiens) [Search protein sequence]
QRKLEALIRDPRSPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYE
KIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKF
EMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGD
LVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHG
HLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGFYGRECD
WWSVGVFLYEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAEISKHAK
NLICAFLTDREVRLGRNGVEEIRQHPFFKNDQWHWDNIRETAAPVVPELS
SDIDSSNFDDIEDDVETFPIPKAFVGNQLPFIGFTYYR
3D structure
PDB4l6q Linking phenotype to kinase: identification of a novel benzoxaborole hinge-binding motif for kinase inhibition and development of high-potency rho kinase inhibitors.
ChainB
Resolution2.79 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D214 K216 N219 D232 T253
Catalytic site (residue number reindexed from 1) D188 K190 N193 D206 T227
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 1WU B I98 V106 A119 K121 M169 E170 Y171 M172 N219 L221 D232 F384 I72 V80 A93 K95 M143 E144 Y145 M146 N193 L195 D206 F358
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:4l6q, PDBe:4l6q, PDBj:4l6q
PDBsum4l6q
PubMed24049062
UniProtO75116|ROCK2_HUMAN Rho-associated protein kinase 2 (Gene Name=ROCK2)

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