Structure of PDB 4yve Chain A

Receptor sequence
>4yveA (length=390) Species: 9606 (Homo sapiens) [Search protein sequence]
SFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNF
LSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMK
LLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY
MPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML
LDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSGYYGREC
DWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEA
KNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDL
SSDIDTSNFDDLEETFPIPKAFVGNQLPFVGFTYYSNRRY
3D structure
PDB4yve Design, Synthesis, and Structure-Activity Relationships of Pyridine-Based Rho Kinase (ROCK) Inhibitors.
ChainA
Resolution3.4 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 4KK A G85 G88 E89 V90 A103 K105 L107 M153 M156 A215 D216 G80 G83 E84 V85 A98 K100 L102 M148 M151 A210 D211 PDBbind-CN: -logKd/Ki=7.00,Ki=100nM
BindingDB: Ki=100nM
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:4yve, PDBe:4yve, PDBj:4yve
PDBsum4yve
PubMed26039570
UniProtQ13464|ROCK1_HUMAN Rho-associated protein kinase 1 (Gene Name=ROCK1)

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