Structure of PDB 5hvu Chain B

Receptor sequence
>5hvuB (length=394) Species: 9606 (Homo sapiens) [Search protein sequence]
MSFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDN
FLSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAM
KLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME
YMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNM
LLDKSGHLKLADFGTCMKMNKEGMVRCDTPDYISPEVLKSQGGDGYYGRE
CDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKE
AKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPD
LSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYSN
3D structure
PDB5hvu ROCK inhibitors 2. Improving potency, selectivity and solubility through the application of rationally designed solubilizing groups.
ChainB
Resolution2.8 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 T229
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 65R B I82 F87 G88 V90 A103 K105 D117 F120 Y155 M156 A215 D216 I78 F83 G84 V86 A99 K101 D113 F116 Y151 M152 A211 D212 BindingDB: Ki=13nM,IC50=7.0nM
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:5hvu, PDBe:5hvu, PDBj:5hvu
PDBsum5hvu
PubMed29945794
UniProtQ13464|ROCK1_HUMAN Rho-associated protein kinase 1 (Gene Name=ROCK1)

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