Structure of PDB 4yvc Chain A

Receptor sequence
>4yvcA (length=388) Species: 9606 (Homo sapiens) [Search protein sequence]
SFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNF
LSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMK
LLSKFEMIKFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGD
LVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG
HLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECD
WWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAK
NLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLS
SDIDTSNFDDLETFPIPKAFVGNQLPFVGFTYYSNRRY
3D structure
PDB4yvc Design, Synthesis, and Structure-Activity Relationships of Pyridine-Based Rho Kinase (ROCK) Inhibitors.
ChainA
Resolution3.2 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) 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 4KH A I82 G83 R84 F87 V90 A103 K105 M153 M156 D216 I77 G78 R79 F82 V85 A98 K100 M143 M146 D206 PDBbind-CN: -logKd/Ki=5.96,Ki=1.1uM
BindingDB: Ki=1100nM
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:4yvc, PDBe:4yvc, PDBj:4yvc
PDBsum4yvc
PubMed26039570
UniProtQ13464|ROCK1_HUMAN Rho-associated protein kinase 1 (Gene Name=ROCK1)

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