Structure of PDB 4yvc Chain B

Receptor sequence
>4yvcB (length=392) Species: 9606 (Homo sapiens) [Search protein sequence]
MSFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDN
FLSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAM
KLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME
YMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNM
LLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGY
YGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDND
ISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAP
VVPDLSSDIDTSNFDDLEETFPIPKAFVGNQLPFVGFTYYSN
3D structure
PDB4yvc Design, Synthesis, and Structure-Activity Relationships of Pyridine-Based Rho Kinase (ROCK) Inhibitors.
ChainB
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) D194 K196 N199 D212 T233
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 B I82 R84 F87 V90 A103 K105 M153 M156 D216 I78 R80 F83 V86 A99 K101 M149 M152 D212 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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