Structure of PDB 3tv7 Chain D

Receptor sequence
>3tv7D (length=397) Species: 9606 (Homo sapiens) [Search protein sequence]
SFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNF
LSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMK
LLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY
MPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML
LDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYY
GRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDI
SKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPV
VPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYSN
3D structure
PDB3tv7 Pyridylthiazole-based ureas as inhibitors of Rho associated protein kinases (ROCK1 and 2).
ChainD
Resolution2.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D198 K200 N203 D216 T237
Catalytic site (residue number reindexed from 1) D193 K195 N198 D211 T232
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 07Q D G85 F87 G88 E89 V90 A103 K105 L107 M153 M156 D216 G80 F82 G83 E84 V85 A98 K100 L102 M148 M151 D211 BindingDB: IC50=30nM
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:3tv7, PDBe:3tv7, PDBj:3tv7
PDBsum3tv7
PubMed23275831
UniProtQ13464|ROCK1_HUMAN Rho-associated protein kinase 1 (Gene Name=ROCK1)

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